PDBe 2y3i

X-ray diffraction
2.9Å resolution

The structure of the fully closed conformation of human PGK in complex with L-ADP, 3PG and the TSA aluminium tetrafluoride

Released:

Function and Biology Details

Reaction catalysed:
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglycerate kinase 1 Chains: A, D
Molecule details ›
Chains: A, D
Length: 416 amino acids
Theoretical weight: 44.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P00558 (Residues: 1-416; Coverage: 100%)
  • Best match: P00558-2 (Residues: 1-388)
Gene names: MIG10, OK/SW-cl.110, PGK1, PGKA
Sequence domains: Phosphoglycerate kinase
Structure domains: Rossmann fold

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 38.419Å b: 103.877Å c: 203.094Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.265 0.263 0.303
Expression system: Escherichia coli BL21