Structure of PDB 1yjx Chain K

Receptor sequence
>1yjxK (length=239) Species: 9606 (Homo sapiens) [Search protein sequence]
AYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYEF
DICFTSVQKRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAE
TAAKHGEAQVKIWRRSYDVPPPPMEPDHPFYSNISKDRRYADLTEDQLPS
CESLKDTIARALPFWNEEIVPQIKEGKRVLIAAHGNSLRGIVKHLEGLSE
EAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVRK
3D structure
PDB1yjx Crystal structure of human B-type phosphoglycerate mutase bound with citrate.
ChainK
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H11 R62 E89 H186
Catalytic site (residue number reindexed from 1) H9 R60 E87 H184
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 CL K V81 R83 V79 R81
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:1yjx, PDBe:1yjx, PDBj:1yjx
PDBsum1yjx
PubMed15883004
UniProtP18669|PGAM1_HUMAN Phosphoglycerate mutase 1 (Gene Name=PGAM1)

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