› 5uaw

X-ray diffraction
1.85Å resolution

Structure of apo human PYCR-1 crystallized in space group P21212

Released:
DOI: 10.2210/pdb5uaw/pdb
PDB entry 5uaw coloured by chain, front view.
PDB entry 5uaw coloured by chain, side view.
PDB entry 5uaw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1.
Christensen EM, Patel SM, Korasick DA, Campbell AC, Krause KL, Becker DF, Tanner JJ
J Biol Chem 292 7233-7243 (2017)
PMID: 28258219

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:
homo decamer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152260 (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: 322 amino acids
Theoretical weight: 34.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P32322 (Residues: 1-300; Coverage: 94%)
Gene name: PYCR1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P21212
Unit cell:
a: 163.03Å b: 88.14Å c: 117.32Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.216
Expression system: Escherichia coli

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Citations

9 review citations

Proline Metabolism in Cell Regulation and Cancer Biology: Recent Advances and Hypotheses.
Phang JM. (2019)
8 more

1 mention without citation

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