Structure of PDB 7xb7 Chain C

Receptor sequence
>7xb7C (length=236) Species: 9606 (Homo sapiens) [Search protein sequence]
AYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYEF
DICFTSVQKRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAE
TAAKHGEAQVKIWRRSYDVPPPPMEPDHPFYSNISKDRRYADLTEDQLPS
CESLKDTIARALPFWNEEIVPQIKEGKRVLIAAHGNSLRGIVKHLEGLSE
EAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEET
3D structure
PDB7xb7 Phosphoglycerate mutase 1 complexed with a covalent inhibitor
ChainC
Resolution2.2 Å
3D
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Enzymatic activity
Enzyme Commision number 5.4.2.11: phosphoglycerate mutase (2,3-diphosphoglycerate-dependent).
5.4.2.4: bisphosphoglycerate mutase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CKF C F22 E89 R90 Y92A K100 V112 W115 R116 N188 F20 E87 R88 Y90 K98 V110 W113 R114 N186
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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Cellular Component
External links
PDB RCSB:7xb7, PDBe:7xb7, PDBj:7xb7
PDBsum7xb7
PubMed
UniProtP18669|PGAM1_HUMAN Phosphoglycerate mutase 1 (Gene Name=PGAM1)

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