Structure of PDB 1hdi Chain A

Receptor sequence

>1hdiA (length=413) Species: 9823 (Sus scrofa)

NKLTLDKLNVKGKRVVMRVDFNVPMAAAQITNNARIKAAVPSIKFCLDDG
AKSVVLMSHLGRPDGSPMPDKYSLQPVAAELKSALGKAVLFLKDCVGPAV
EKACADPAAGSVILLENLRFHVEEEGKGKDASGNKAAGEPAKIKAFRASL
SALGDVYVNDAFGTAHRAHSSMVGVNLPKKAGAFLMKKELNYFAAAAESP
ERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGMAFTFLKVLNNMEIG
TSLFDEAGKKIVKNLMSKAAANGVKITLPVDFVTADKFDEQAKIGQATVA
SGIPAGWMGLDCGPKSSAKYSEAVARAKQIVWNGPVGVFEWEAFAQGTKA
LMDEVVKATSRGCITIIGGGDTATCCAKWNTEDNVSHVSTGGGASLELLE
GKVLPGVDALSNV

3D structure

• PDB: 1hdi A 1.8 A resolution structure of pig muscle 3-phosphoglycerate kinase with bound MgADP and 3-phosphoglycerate in open conformation: new insight into the role of the nucleotide in domain closure.
• Chain: A
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R38 K215 G373 G396
• Catalytic site (residue number reindexed from 1): R35 K212 G370 G393
• Enzyme Commision number: 2.7.2.3: phosphoglycerate kinase.

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	AMP	A	A214 G237 G238 L313 G340 V341 E343 D374	A211 G234 G235 L310 G337 V338 E340 D371

Gene Ontology

Molecular Function

• GO:0004618 phosphoglycerate kinase activity
• GO:0005524 ATP binding
• GO:0016301 kinase activity
• GO:0043531 ADP binding

Biological Process

• GO:0006094 gluconeogenesis
• GO:0006096 glycolytic process
• GO:0016310 phosphorylation

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:1hdi, PDBe:1hdi, PDBj:1hdi
• PDBsum: 1hdi
• PubMed: 11178909
• UniProt: Q7SIB7|PGK1_PIG Phosphoglycerate kinase 1 (Gene Name=PGK1)