HEADER TRANSFERASE 20-JUL-09 3ID8
TITLE TERNARY COMPLEX OF HUMAN PANCREATIC GLUCOKINASE CRYSTALLIZED WITH
TITLE 2 ACTIVATOR, GLUCOSE AND AMP-PNP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOKINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 12-465;
COMPND 5 SYNONYM: HEXOKINASE TYPE IV, HK IV, HEXOKINASE-4, HK4, HEXOKINASE-D;
COMPND 6 EC: 2.7.1.2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS GLUCOKINASE, HEXOKINASE IV, ATP-BINDING, DIABETES MELLITUS, DISEASE
KEYWDS 2 MUTATION, GLYCOLYSIS, KINASE, NUCLEOTIDE-BINDING, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.PETIT,L.GLUAIS,A.LAGARDE,J.A.BOUTIN,G.FERRY,L.VUILLARD
REVDAT 5 01-NOV-23 3ID8 1 HETSYN
REVDAT 4 29-JUL-20 3ID8 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 SITE
REVDAT 3 25-APR-12 3ID8 1 JRNL
REVDAT 2 09-NOV-11 3ID8 1 JRNL VERSN
REVDAT 1 28-JUL-10 3ID8 0
JRNL AUTH P.PETIT,M.ANTOINE,G.FERRY,J.A.BOUTIN,A.LAGARDE,L.GLUAIS,
JRNL AUTH 2 R.VINCENTELLI,L.VUILLARD
JRNL TITL THE ACTIVE CONFORMATION OF HUMAN GLUCOKINASE IS NOT ALTERED
JRNL TITL 2 BY ALLOSTERIC ACTIVATORS
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 67 929 2011
JRNL REFN ISSN 0907-4449
JRNL PMID 22101819
JRNL DOI 10.1107/S0907444911036729
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 18338
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 966
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1321
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2270
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.3040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3535
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 68
REMARK 3 SOLVENT ATOMS : 125
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.92000
REMARK 3 B22 (A**2) : 1.03000
REMARK 3 B33 (A**2) : -1.94000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.521
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.308
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.899
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3684 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4962 ; 1.513 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 454 ; 5.864 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 177 ;37.087 ;23.898
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 675 ;18.651 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;19.341 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 541 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2761 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1690 ; 0.230 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2443 ; 0.300 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 172 ; 0.177 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.203 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 29 ; 0.244 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.399 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2227 ; 0.612 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3575 ; 1.158 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1457 ; 1.625 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1384 ; 2.698 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3ID8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1000054265.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18612
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 19.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : 0.08000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.42000
REMARK 200 R SYM FOR SHELL (I) : 0.39000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1V4S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 33.50000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.40000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.30000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.40000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.50000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.30000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -4
REMARK 465 GLY A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 GLU A 4
REMARK 465 GLU A 95
REMARK 465 GLU A 96
REMARK 465 GLY A 97
REMARK 465 LYS A 458
REMARK 465 LYS A 459
REMARK 465 ALA A 460
REMARK 465 CYS A 461
REMARK 465 MET A 462
REMARK 465 LEU A 463
REMARK 465 GLY A 464
REMARK 465 GLN A 465
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 64 -107.84 -34.25
REMARK 500 GLU A 67 -146.88 -96.41
REMARK 500 LYS A 136 -30.53 -37.75
REMARK 500 GLN A 138 83.75 25.94
REMARK 500 MET A 139 -0.80 -142.14
REMARK 500 HIS A 141 -44.27 -166.61
REMARK 500 ASP A 194 -98.57 5.20
REMARK 500 GLU A 196 99.82 71.34
REMARK 500 ILE A 293 -50.29 -123.24
REMARK 500 SER A 418 -0.89 -149.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 192 0.19 SIDE CHAIN
REMARK 500 ARG A 394 0.24 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 700 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 205 OD1
REMARK 620 2 ANP A 600 O2G 78.1
REMARK 620 3 ANP A 600 O1B 138.6 63.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 800 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 238 O
REMARK 620 2 VAL A 241 O 88.9
REMARK 620 3 VAL A 244 O 141.7 70.1
REMARK 620 4 GLY A 246 O 76.0 145.1 102.9
REMARK 620 N 1 2 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1V4S RELATED DB: PDB
REMARK 900 1V4S WAS OBTAINED WITH A DIFFERENT ISOFORM AT A LOWER PH IN A
REMARK 900 DIFFERENT UNIT CELL
REMARK 900 RELATED ID: 3F9M RELATED DB: PDB
REMARK 900 HUMAN PANCREATIC GLUCOKINASE IN COMPLEX WITH GLUCOSE AND ACTIVATOR
REMARK 900 RELATED ID: 3FGU RELATED DB: PDB
REMARK 900 HUMAN PANCREATIC GLUCOKINASE IN COMPLEX WITH GLUCOSE AND AMP-PNP
REMARK 900 RELATED ID: 3IDH RELATED DB: PDB
REMARK 900 HUMAN PANCREATIC GLUCOKINASE IN COMPLEX WITH GLUCOSE
DBREF 3ID8 A 12 465 UNP P35557 HXK4_HUMAN 12 465
SEQADV 3ID8 MET A -4 UNP P35557 EXPRESSION TAG
SEQADV 3ID8 GLY A -3 UNP P35557 EXPRESSION TAG
SEQADV 3ID8 HIS A -2 UNP P35557 EXPRESSION TAG
SEQADV 3ID8 HIS A -1 UNP P35557 EXPRESSION TAG
SEQADV 3ID8 HIS A 0 UNP P35557 EXPRESSION TAG
SEQADV 3ID8 HIS A 1 UNP P35557 EXPRESSION TAG
SEQADV 3ID8 HIS A 2 UNP P35557 EXPRESSION TAG
SEQADV 3ID8 HIS A 3 UNP P35557 EXPRESSION TAG
SEQADV 3ID8 GLU A 4 UNP P35557 EXPRESSION TAG
SEQADV 3ID8 ASN A 5 UNP P35557 EXPRESSION TAG
SEQADV 3ID8 LEU A 6 UNP P35557 EXPRESSION TAG
SEQADV 3ID8 TYR A 7 UNP P35557 EXPRESSION TAG
SEQADV 3ID8 PHE A 8 UNP P35557 EXPRESSION TAG
SEQADV 3ID8 GLN A 9 UNP P35557 EXPRESSION TAG
SEQADV 3ID8 GLY A 10 UNP P35557 EXPRESSION TAG
SEQADV 3ID8 MET A 11 UNP P35557 EXPRESSION TAG
SEQRES 1 A 470 MET GLY HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE
SEQRES 2 A 470 GLN GLY MET LYS LYS GLU LYS VAL GLU GLN ILE LEU ALA
SEQRES 3 A 470 GLU PHE GLN LEU GLN GLU GLU ASP LEU LYS LYS VAL MET
SEQRES 4 A 470 ARG ARG MET GLN LYS GLU MET ASP ARG GLY LEU ARG LEU
SEQRES 5 A 470 GLU THR HIS GLU GLU ALA SER VAL LYS MET LEU PRO THR
SEQRES 6 A 470 TYR VAL ARG SER THR PRO GLU GLY SER GLU VAL GLY ASP
SEQRES 7 A 470 PHE LEU SER LEU ASP LEU GLY GLY THR ASN PHE ARG VAL
SEQRES 8 A 470 MET LEU VAL LYS VAL GLY GLU GLY GLU GLU GLY GLN TRP
SEQRES 9 A 470 SER VAL LYS THR LYS HIS GLN MET TYR SER ILE PRO GLU
SEQRES 10 A 470 ASP ALA MET THR GLY THR ALA GLU MET LEU PHE ASP TYR
SEQRES 11 A 470 ILE SER GLU CYS ILE SER ASP PHE LEU ASP LYS HIS GLN
SEQRES 12 A 470 MET LYS HIS LYS LYS LEU PRO LEU GLY PHE THR PHE SER
SEQRES 13 A 470 PHE PRO VAL ARG HIS GLU ASP ILE ASP LYS GLY ILE LEU
SEQRES 14 A 470 LEU ASN TRP THR LYS GLY PHE LYS ALA SER GLY ALA GLU
SEQRES 15 A 470 GLY ASN ASN VAL VAL GLY LEU LEU ARG ASP ALA ILE LYS
SEQRES 16 A 470 ARG ARG GLY ASP PHE GLU MET ASP VAL VAL ALA MET VAL
SEQRES 17 A 470 ASN ASP THR VAL ALA THR MET ILE SER CYS TYR TYR GLU
SEQRES 18 A 470 ASP HIS GLN CYS GLU VAL GLY MET ILE VAL GLY THR GLY
SEQRES 19 A 470 CYS ASN ALA CYS TYR MET GLU GLU MET GLN ASN VAL GLU
SEQRES 20 A 470 LEU VAL GLU GLY ASP GLU GLY ARG MET CYS VAL ASN THR
SEQRES 21 A 470 GLU TRP GLY ALA PHE GLY ASP SER GLY GLU LEU ASP GLU
SEQRES 22 A 470 PHE LEU LEU GLU TYR ASP ARG LEU VAL ASP GLU SER SER
SEQRES 23 A 470 ALA ASN PRO GLY GLN GLN LEU TYR GLU LYS LEU ILE GLY
SEQRES 24 A 470 GLY LYS TYR MET GLY GLU LEU VAL ARG LEU VAL LEU LEU
SEQRES 25 A 470 ARG LEU VAL ASP GLU ASN LEU LEU PHE HIS GLY GLU ALA
SEQRES 26 A 470 SER GLU GLN LEU ARG THR ARG GLY ALA PHE GLU THR ARG
SEQRES 27 A 470 PHE VAL SER GLN VAL GLU SER ASP THR GLY ASP ARG LYS
SEQRES 28 A 470 GLN ILE TYR ASN ILE LEU SER THR LEU GLY LEU ARG PRO
SEQRES 29 A 470 SER THR THR ASP CYS ASP ILE VAL ARG ARG ALA CYS GLU
SEQRES 30 A 470 SER VAL SER THR ARG ALA ALA HIS MET CYS SER ALA GLY
SEQRES 31 A 470 LEU ALA GLY VAL ILE ASN ARG MET ARG GLU SER ARG SER
SEQRES 32 A 470 GLU ASP VAL MET ARG ILE THR VAL GLY VAL ASP GLY SER
SEQRES 33 A 470 VAL TYR LYS LEU HIS PRO SER PHE LYS GLU ARG PHE HIS
SEQRES 34 A 470 ALA SER VAL ARG ARG LEU THR PRO SER CYS GLU ILE THR
SEQRES 35 A 470 PHE ILE GLU SER GLU GLU GLY SER GLY ARG GLY ALA ALA
SEQRES 36 A 470 LEU VAL SER ALA VAL ALA CYS LYS LYS ALA CYS MET LEU
SEQRES 37 A 470 GLY GLN
HET GLC A 500 12
HET MRK A 501 23
HET ANP A 600 31
HET MG A 700 1
HET K A 800 1
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM MRK 2-AMINO-4-FLUORO-5-[(1-METHYL-1H-IMIDAZOL-2-YL)
HETNAM 2 MRK SULFANYL]-N-(1,3-THIAZOL-2-YL)BENZAMIDE
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
HETNAM K POTASSIUM ION
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 2 GLC C6 H12 O6
FORMUL 3 MRK C14 H12 F N5 O S2
FORMUL 4 ANP C10 H17 N6 O12 P3
FORMUL 5 MG MG 2+
FORMUL 6 K K 1+
FORMUL 7 HOH *125(H2 O)
HELIX 1 1 LEU A 6 ALA A 21 1 16
HELIX 2 2 GLU A 22 GLN A 24 5 3
HELIX 3 3 GLN A 26 ARG A 46 1 21
HELIX 4 4 ARG A 46 GLU A 51 1 6
HELIX 5 5 PRO A 111 THR A 116 1 6
HELIX 6 6 THR A 118 HIS A 137 1 20
HELIX 7 7 ASN A 180 GLY A 193 1 14
HELIX 8 8 ASN A 204 TYR A 214 1 11
HELIX 9 9 GLN A 239 VAL A 241 5 3
HELIX 10 10 GLU A 256 PHE A 260 5 5
HELIX 11 11 LEU A 266 LEU A 270 5 5
HELIX 12 12 LEU A 271 SER A 280 1 10
HELIX 13 13 TYR A 289 GLY A 294 1 6
HELIX 14 14 GLY A 294 GLU A 312 1 19
HELIX 15 15 LEU A 315 GLU A 319 5 5
HELIX 16 16 GLU A 331 SER A 340 1 10
HELIX 17 17 ARG A 345 THR A 354 1 10
HELIX 18 18 SER A 360 SER A 396 1 37
HELIX 19 19 GLY A 410 HIS A 416 1 7
HELIX 20 20 SER A 418 THR A 431 1 14
HELIX 21 21 GLU A 443 CYS A 457 1 15
SHEET 1 A 6 LEU A 58 ARG A 63 0
SHEET 2 A 6 ARG A 250 ASN A 254 -1 O ASN A 254 N LEU A 58
SHEET 3 A 6 CYS A 230 GLU A 237 -1 N GLU A 236 O MET A 251
SHEET 4 A 6 CYS A 220 VAL A 226 -1 N GLY A 223 O CYS A 233
SHEET 5 A 6 MET A 402 ASP A 409 1 O GLY A 407 N MET A 224
SHEET 6 A 6 CYS A 434 GLU A 440 1 O ILE A 439 N VAL A 406
SHEET 1 B 5 TRP A 99 SER A 109 0
SHEET 2 B 5 ASN A 83 GLY A 92 -1 N VAL A 86 O GLN A 106
SHEET 3 B 5 GLY A 72 LEU A 79 -1 N SER A 76 O MET A 87
SHEET 4 B 5 PRO A 145 PHE A 150 1 O THR A 149 N LEU A 79
SHEET 5 B 5 ASP A 198 VAL A 203 1 O ASP A 198 N LEU A 146
SHEET 1 C 2 VAL A 154 ASP A 158 0
SHEET 2 C 2 LYS A 161 LEU A 164 -1 O LYS A 161 N GLU A 157
LINK OD1 ASP A 205 MG MG A 700 1555 1555 2.42
LINK O MET A 238 K K A 800 1555 1555 2.68
LINK O VAL A 241 K K A 800 1555 1555 2.90
LINK O VAL A 244 K K A 800 1555 1555 2.65
LINK O GLY A 246 K K A 800 1555 1555 2.49
LINK O2G ANP A 600 MG MG A 700 1555 1555 2.33
LINK O1B ANP A 600 MG MG A 700 1555 1555 2.89
CISPEP 1 ASP A 194 PHE A 195 0 9.70
CRYST1 67.000 82.600 86.800 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014925 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012107 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011521 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
