2gra

X-ray diffraction
3.1Å resolution

crystal structure of Human Pyrroline-5-carboxylate Reductase complexed with nadp

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of human pyrroline-5-carboxylate reductase.
J Mol Biol 359 1364-77 (2006)
PMID: 16730026

Function and Biology Details

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
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: 277 amino acids
Theoretical weight: 29.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P32322 (Residues: 1-275; Coverage: 86%)
Gene name: PYCR1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 5 x NAP
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: C2
Unit cell:
a: 207.868Å b: 123.502Å c: 120.826Å
α: 90° β: 121.97° γ: 90°
R-values:
R R work R free
0.232 0.228 0.249
Expression system: Escherichia coli