Structure of PDB 1kf0 Chain A

Receptor sequence
>1kf0A (length=416) Species: 9823 (Sus scrofa) [Search protein sequence]
SLSNKLTLDKLNVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCL
DDGAKSVVLMSHLGRPDGSPMPDKYSLQPVAVELKSLLGKDVLFLKDCVG
PEVEKACADPAAGSVILLENLRFHVEEEGKGKDASGNKVKAEPAKIKTFR
ASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPKKAGGFLMKKELNYFAKAL
ESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGMAFTFLKVLNNM
EIGTSLFDEEGAKIVKNLMSKAEKNGVKITLPVDFVTADKFDEHAKTGQA
TVASGIPAGWMGLDCGPESSKKYSEAVARAKQIVWNGPVGVFEWEAFAQG
TKALMDEVVKATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLE
LLEGKVLPGVDALSNV
3D structure
PDB1kf0 Crystallographic and thiol-reactivity studies on the complex of pig muscle phosphoglycerate kinase with ATP analogues: correlation between nucleotide binding mode and helix flexibility.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R38 K215 G373 G396
Catalytic site (residue number reindexed from 1) R38 K215 G373 G396
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 ACP A G213 A214 G237 G238 G340 V341 E343 G213 A214 G237 G238 G340 V341 E343 MOAD: Kd=2.8mM
PDBbind-CN: -logKd/Ki=2.55,Kd=2.80mM
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1kf0, PDBe:1kf0, PDBj:1kf0
PDBsum1kf0
PubMed12102622
UniProtQ7SIB7|PGK1_PIG Phosphoglycerate kinase 1 (Gene Name=PGK1)

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