PDBe 2x13

X-ray diffraction
1.74Å resolution

The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with ADP and 3phosphoglycerate

Released:
Source organism: Homo sapiens
Entry authors: Bowler MW, Cliff MJ, Marston JPM, Baxter NJ, Hownslow AMH, Varga AV, Szabo J, Vas M, Blackburn GM, Waltho JP

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 Chain: A
Molecule details ›
Chain: A
Length: 416 amino acids
Theoretical weight: 44.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P00558 (Residues: 2-417; Coverage: 100%)
Gene names: MIG10, OK/SW-cl.110, PGK1, PGKA
Sequence domains: Phosphoglycerate kinase
Structure domains: Rossmann fold

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 38.94Å b: 91.44Å c: 108.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.185 0.218
Expression system: Escherichia coli BL21