› 6xp0

X-ray diffraction
1.95Å resolution

Structure of human PYCR1 complexed with N-formyl L-proline

Released:
DOI: 10.2210/pdb6xp0/pdb
PDB entry 6xp0 coloured by chain, front view.
PDB entry 6xp0 coloured by chain, side view.
PDB entry 6xp0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
In crystallo screening for proline analog inhibitors of the proline cycle enzyme PYCR1.
Christensen EM, Bogner AN, Vandekeere A, Tam GS, Patel SM, Becker DF, Fendt SM, Tanner JJ
J Biol Chem 295 18316-18327 (2020)
PMID: 33109600

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

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152259 (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:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21212
Unit cell:
a: 164.63Å b: 88.513Å c: 115.462Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.209
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Targeting cancer metabolism in the era of precision oncology.
Stine et al. (2022)
6 more

2 mentions without citation

In crystallo screening for proline analog inhibitors of the proline cycle enzyme PYCR1.
Christensen et al. (2020)
1 more