Structure of PDB 1yfk Chain A

Receptor sequence

>1yfkA (length=243) Species: 9606 (Homo sapiens)

AYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYEF
DICFTSVQKRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAE
TAAKHGEAQVKIWRRSYDVPPPPMEPDHPFYSNISKDRRYADLTEDQLPS
CESLKDTIARALPFWNEEIVPQIKEGKRVLIAAHGNSLRGIVKHLEGLSE
EAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVRKAMEA

3D structure

• PDB: 1yfk Crystal structure of human B-type phosphoglycerate mutase bound with citrate.
• Chain: A
• Resolution: 2.7 Å

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	A	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

External links

• PDB: RCSB:1yfk, PDBe:1yfk, PDBj:1yfk
• PDBsum: 1yfk
• PubMed: 15883004
• UniProt: P18669|PGAM1_HUMAN Phosphoglycerate mutase 1 (Gene Name=PGAM1)