Structure of PDB 8it8 Chain C

Receptor sequence

>8it8C (length=240) Species: 9606 (Homo sapiens)

AAYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYE
FDICFTSVQKRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKA
ETAAKHGEAQVKIWRRSYDVPPPPMEPDHPFYSNISKDRRYADLTEDQLP
SCESLKDTIARALPFWNEEIVPQIKEGKRVLIAAHGNSLRGIVKHLEGLS
EEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVRK

3D structure

• PDB: 8it8 Phosphoglycerate mutase 1 complexed with a compound
• Chain: C
• Resolution: 1.95 Å

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	Q9L	C	N17 N20 R21 F22 R90 K100 R116	N16 N19 R20 F21 R89 K99 R115

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:8it8, PDBe:8it8, PDBj:8it8
• PDBsum: 8it8
• UniProt: P18669|PGAM1_HUMAN Phosphoglycerate mutase 1 (Gene Name=PGAM1)