Structure of PDB 1dqr Chain A Binding Site BS01

Receptor Information
>1dqr Chain A (length=555) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AALTRNPQFQKLQQWHREHGSELNLRHLFDTDKERFNHFSLTLNTNHGHI
LLDYSKNLVTEEVMHMLLDLAKSRGVEAARESMFNGEKINSTEDRAVLHV
ALRNRSNTPIVVDGKDVMPEVNKVLDKMKAFCQRVRSGDWKGYTGKTITD
VINIGIGGSDLGPLMVTEALKPYSSGGPRVWFVSNIDGTHIAKTLACLNP
ESSLFIIASKTFTTQETITNAKTAKDWFLLSAKDPSTVAKHFVALSTNTA
KVKEFGIDPQNMFEFWDWVGGRYSLWSAIGLSIALHVGFDNFEQLLSGAH
WMDQHFRTTPLEKNAPVLLAMLGIWYINCFGCETQAVLPYDQYLHRFAAY
FQQGDMESNGKYITKSGARVDHQTGPIVWGEPGTNGQHAFYQLIHQGTKM
IPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMKGKSTEEARKELQA
AGKSPEDLMKLLPHKVFEGNRPTNSIVFTKLTPFILGALIAMYEHKIFVQ
GVVWDINSFDQWGVELGKQLAKKIEPELDGSSPVTSHDSSTNGLINFIKQ
QREAK
Ligand information
Ligand ID6PG
InChIInChI=1S/C6H13O10P/c7-2(1-16-17(13,14)15)3(8)4(9)5(10)6(11)12/h2-5,7-10H,1H2,(H,11,12)(H2,13,14,15)/t2-,3-,4+,5-/m1/s1
InChIKeyBIRSGZKFKXLSJQ-SQOUGZDYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@H](O)[C@@H](O)C(O)=O
OpenEye OEToolkits 1.5.0C([C@H]([C@H]([C@@H]([C@H](C(=O)O)O)O)O)O)OP(=O)(O)O
ACDLabs 10.04O=P(O)(O)OCC(O)C(O)C(O)C(O)C(=O)O
OpenEye OEToolkits 1.5.0C(C(C(C(C(C(=O)O)O)O)O)O)OP(=O)(O)O
CACTVS 3.341O[CH](CO[P](O)(O)=O)[CH](O)[CH](O)[CH](O)C(O)=O
FormulaC6 H13 O10 P
Name6-PHOSPHOGLUCONIC ACID
ChEMBLCHEMBL1230513
DrugBankDB02076
ZINCZINC000001532623
PDB chain1dqr Chain A Residue 600 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1dqr Crystal structure of rabbit phosphoglucose isomerase, a glycolytic enzyme that moonlights as neuroleukin, autocrine motility factor, and differentiation mediator.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		G157 G158 S159 S209 K210 T211 T214 G271 R272 Q353
Binding residue
(residue number reindexed from 1)		G157 G158 S159 S209 K210 T211 T214 G271 R272 Q353
Annotation score1
Binding affinityMOAD: Ki=43uM
Enzymatic activity
Catalytic site (original residue number in PDB) K210 E216 G271 R272 E357 H388 K518
Catalytic site (residue number reindexed from 1) K210 E216 G271 R272 E357 H388 K518
Enzyme Commision number 5.3.1.9: glucose-6-phosphate isomerase.
Gene Ontology
Molecular Function
GO:0004347 glucose-6-phosphate isomerase activity
GO:0005125 cytokine activity
GO:0016853 isomerase activity
GO:0048029 monosaccharide binding
GO:0097367 carbohydrate derivative binding
Biological Process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0007165 signal transduction
GO:0051156 glucose 6-phosphate metabolic process
GO:1901135 carbohydrate derivative metabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1dqr, PDBe:1dqr, PDBj:1dqr
PDBsum1dqr
PubMed10653639
UniProtQ9N1E2|G6PI_RABIT Glucose-6-phosphate isomerase (Gene Name=GPI)

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