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Structure of PDB 1vjd Chain A

Receptor sequence >1vjdA (length=416) Species: 9823 (Sus scrofa) [Search protein sequence] SLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAIPSIKFCL DNGAKSVVLMSHLGRPDGIPMPDKYSLEPVAVELKSLLGKDVLFLKDCVG PEVEKACADPAAGSVILLENLRFHVEEEGKGKDASGSKVKADPAKIEAFR ASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPKKAGGFLMKKELNYFAKAL ESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGMAFTFLKVLNNM EIGTSLFDEEGSKIVKDLMSKAEKNGVKITLPVDFVTADKFDENAKTGQA TVASGIPAGWMGLDCGPESSKKYSEAVARAKQIVWNGPVGVFEWEAFAQG TKALMDEVVKATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLE LLEGKVLPGVDALSNV

3D structure PDB 1vjd Role of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: binding, kinetic, and crystallographic studies with ATP and MgATP. Chain A Resolution 1.9 Å 3D structure Catalytic site residues are labeled in the structure [Spin on] [Spin off] [Reset orientation] [High quality] [Low quality] [White background] [Black background] [Download] [Download structure with residue number starting from 1]

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 ATP A G213 A214 K219 G237 G238 G312 G337 P338 G340 V341 E343 G372 G373 D374 T375 G213 A214 K219 G237 G238 G312 G337 P338 G340 V341 E343 G372 G373 D374 T375 MOAD: Kd=0.286mM PDBbind-CN: -logKd/Ki=3.54,Kd=0.286mM

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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