Structure of PDB 1zmr Chain A

Receptor sequence

>1zmrA (length=386) Species: 562 (Escherichia coli)

SVIKMTDLDLAGKRVFIRADLNVPVKDGKVTSDARIRASLPTIELALKQG
AKVMVTSHLGRPTEGEYNEEFSLLPVVNYLKDKLSNPVRLVKDYLDGVDV
AEGELVVLENVRFNKGEKKDDETLSKKYAALCDVFVMDAFGTAHRAQAST
HGIGKFADVACAGPLLAAELDALGKALKEPARPMVAIVGGSKVSTKLTVL
DSLSKIADQLIVGGGIANTFIAAQGHDVGKSLYEADLVDEAKRLLTTCNI
PVPSDVRVATEFSETAPATLKSVNDVKADEQILDIGDASAQELAEILKNA
KTILWNGPVGVFEFPNFRKGTEIVANAIADSEAFSIAGGGDTLAAIDLFG
IADKISYISTGGGAFLEFVEGKVLPAVAMLEERAKK

3D structure

• PDB: 1zmr Comparison of proteolytic susceptibility in phosphoglycerate kinases from yeast and E. coli: modulation of conformational ensembles without altering structure or stability.
• Chain: A
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R36 K193 G341 G364
• Catalytic site (residue number reindexed from 1): R35 K192 G340 G363
• 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	CA	A	D237 D240	D236 D239
BS02	CA	A	K82 L85	K81 L84

Gene Ontology

Molecular Function

• GO:0004618 phosphoglycerate kinase activity
• GO:0005524 ATP binding
• GO:0016301 kinase activity
• GO:0043531 ADP binding
• GO:0097216 guanosine tetraphosphate 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:1zmr, PDBe:1zmr, PDBj:1zmr
• PDBsum: 1zmr
• PubMed: 17397866
• UniProt: P0A799|PGK_ECOLI Phosphoglycerate kinase (Gene Name=pgk)