› 3c39

X-ray diffraction
1.85Å resolution

Crystal Structure of human phosphoglycerate kinase bound to 3-phosphoglycerate

Released:
DOI: 10.2210/pdb3c39/pdb
PDB entry 3c39 coloured by chain, front view.
PDB entry 3c39 coloured by chain, side view.
PDB entry 3c39 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular basis for the lack of enantioselectivity of human 3-phosphoglycerate kinase.
Gondeau C, Chaloin L, Lallemand P, Roy B, Périgaud C, Barman T, Varga A, Vas M, Lionne C, Arold ST
Nucleic Acids Res 36 3620-9 (2008)
PMID: 18463139

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132717 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglycerate kinase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 420 amino acids
Theoretical weight: 44.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00558 (Residues: 1-417; Coverage: 100%)
Gene names: MIG10, OK/SW-cl.110, PGK1, PGKA
Sequence domains: Phosphoglycerate kinase
Structure domains: Phosphoglycerate kinase, N-terminal domain

Ligands and Environments

1 bound ligand:
Ligand 3PG 2 x 3PG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P1
Unit cell:
a: 35.616Å b: 55.79Å c: 93.23Å
α: 79.18° β: 84.33° γ: 83.23°
R-values:
R R work R free
0.194 0.191 0.273
Expression system: Escherichia coli

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Citations

1 review citation

Conformational dynamics in phosphoglycerate kinase, an open and shut case?
Bowler MW. (2013)
19 other articles

7 mentions without citation

Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids.
Liberta et al. (2019)
6 more