› 3tri

X-ray diffraction
2.5Å resolution

Structure of a pyrroline-5-carboxylate reductase (proC) from Coxiella burnetii

Released:
DOI: 10.2210/pdb3tri/pdb
PDB entry 3tri coloured by chain, front view.
PDB entry 3tri coloured by chain, side view.
PDB entry 3tri coloured by chain, top view.
Source organism: Coxiella burnetii
Primary publication:
Structural genomics for drug design against the pathogen Coxiella burnetii.
Franklin MC, Cheung J, Rudolph MJ, Burshteyn F, Cassidy M, Gary E, Hillerich B, Yao ZK, Carlier PR, Totrov M, Love JD
Proteins 83 2124-36 (2015)
PMID: 26033498

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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182890 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyrroline-5-carboxylate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 280 amino acids
Theoretical weight: 30.76 KDa
Source organism: Coxiella burnetii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q83A21 (Residues: 1-274; Coverage: 100%)
Gene names: CBU_2090, proC
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 2 x NAP
2 bound ligands:
Ligand PO4 4 x PO4
Ligand CL 1 x CL
1 modified residue:
Ligand MSE 14 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P65
Unit cell:
a: 75.411Å b: 75.411Å c: 189.234Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.182 0.235
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology.
Martins et al. (2015)
3 more

2 mentions without citation

Comparison of N-glycosides of fetuins from different species and human alpha 2-HS-glycoprotein.
Hayase et al. (1992)
1 more