Structure of PDB 1yjx Chain L Binding Site BS01

Receptor Information
>1yjx Chain L (length=245) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AAYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYE
FDICFTSVQKRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKA
ETAAKHGEAQVKIWRRSYDVPPPPMEPDHPFYSNISKDRRYADLTEDQLP
SCESLKDTIARALPFWNEEIVPQIKEGKRVLIAAHGNSLRGIVKHLEGLS
EEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVRKAMEAV
Ligand information
Ligand IDCL
InChIInChI=1S/ClH/h1H/p-1
InChIKeyVEXZGXHMUGYJMC-UHFFFAOYSA-M
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Cl-]
FormulaCl
NameCHLORIDE ION
ChEMBL
DrugBankDB14547
ZINC
PDB chain1yjx Chain K Residue 263 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1yjx Crystal structure of human B-type phosphoglycerate mutase bound with citrate.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		V81 R83
Binding residue
(residue number reindexed from 1)		V80 R82
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H11 R62 E89 H186
Catalytic site (residue number reindexed from 1) H10 R61 E88 H185
Enzyme Commision number 5.4.2.11: phosphoglycerate mutase (2,3-diphosphoglycerate-dependent).
5.4.2.4: bisphosphoglycerate mutase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004082 bisphosphoglycerate mutase activity
GO:0004619 phosphoglycerate mutase activity
GO:0005515 protein binding
GO:0016787 hydrolase activity
GO:0016853 isomerase activity
GO:0016868 intramolecular phosphotransferase activity
GO:0019901 protein kinase binding
GO:0046538 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
Biological Process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0061621 canonical glycolysis
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016020 membrane
GO:0034774 secretory granule lumen
GO:0070062 extracellular exosome
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1yjx, PDBe:1yjx, PDBj:1yjx
PDBsum1yjx
PubMed15883004
UniProtP18669|PGAM1_HUMAN Phosphoglycerate mutase 1 (Gene Name=PGAM1)

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