› 2ger

X-ray diffraction
3.1Å resolution

Crystal Structure and Oxidative Mechanism of Human Pyrroline-5-carboxylate Reductase

Released:
DOI: 10.2210/pdb2ger/pdb
PDB entry 2ger coloured by chain, front view.
PDB entry 2ger coloured by chain, side view.
PDB entry 2ger coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human pyrroline-5-carboxylate reductase.
Meng Z, Lou Z, Liu Z, Li M, Zhao X, Bartlam M, Rao Z
J Mol Biol 359 1364-77 (2006)
PMID: 16730026

Function and Biology Details

Reaction catalysed: 
L-proline + NAD(P)(+) = 1-pyrroline-5-carboxylate + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-152258 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyrroline-5-carboxylate reductase 1, mitochondrial Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 321 amino acids
Theoretical weight: 33.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P32322 (Residues: 1-319; Coverage: 100%)
Gene name: PYCR1
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 207.607Å b: 123.805Å c: 120.79Å
α: 90° β: 121.76° γ: 90°
R-values:
R R work R free
0.24 0.233 0.261
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Proline mechanisms of stress survival.
Liang et al. (2013)
8 more

3 mentions without citation

Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1.
Christensen et al. (2017)
2 more