› 1hdi

X-ray diffraction
1.8Å resolution

Pig muscle 3-PHOSPHOGLYCERATE KINASE complexed with 3-PG and MgADP.

Released:
DOI: 10.2210/pdb1hdi/pdb
PDB entry 1hdi coloured by chain, front view.
PDB entry 1hdi coloured by chain, side view.
PDB entry 1hdi coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
A 1.8 A resolution structure of pig muscle 3-phosphoglycerate kinase with bound MgADP and 3-phosphoglycerate in open conformation: new insight into the role of the nucleotide in domain closure.
Szilágyi AN, Ghosh M, Garman E, Vas M
J Mol Biol 306 499-511 (2001)
PMID: 11178909

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181945 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglycerate kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 413 amino acids
Theoretical weight: 43.4 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: Q7SIB7 (Residues: 5-417; Coverage: 99%)
Gene name: PGK1
Sequence domains: Phosphoglycerate kinase
Structure domains: Phosphoglycerate kinase, N-terminal domain

Ligands and Environments

3 bound ligands:
Ligand AMP 1 x AMP
Ligand MG 1 x MG
Ligand 3PG 1 x 3PG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX7.2
Spacegroup: P21
Unit cell:
a: 50.5Å b: 105.2Å c: 35.9Å
α: 90° β: 98.4° γ: 90°
R-values:
R R work R free
0.207 0.207 0.262

Quick links

Citations

1 review citation

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

2 mentions without citation

"Hot cores" in proteins: comparative analysis of the apolar contact area in structures from hyper/thermophilic and mesophilic organisms.
Paiardini et al. (2008)
1 more