› 3gt0

X-ray diffraction
2Å resolution

Crystal structure of pyrroline 5-carboxylate reductase from Bacillus cereus. Northeast Structural Genomics Consortium Target BcR38B

Released:
DOI: 10.2210/pdb3gt0/pdb
PDB entry 3gt0 coloured by chain, front view.
PDB entry 3gt0 coloured by chain, side view.
PDB entry 3gt0 coloured by chain, top view.
Source organism: Bacillus cereus ATCC 14579
Entry authors: Kuzin AP, Abashidze M, Seetharaman J, Shastry R, Fang Y, Cunningham K, Ma L-C, Xiao R, Liu J, Baran MC, Acton TB, Rost B, Montelione GT, Tong L, Hunt JF, Northeast Structural Genomics Consortium (NESG)

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 dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-182486 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyrroline-5-carboxylate reductase Chain: A
Molecule details ›
Chain: A
Length: 247 amino acids
Theoretical weight: 26.95 KDa
Source organism: Bacillus cereus ATCC 14579
Expression system: Escherichia coli
UniProt:
  • Canonical: Q81C08 (Residues: 1-247; Coverage: 91%)
Gene names: BC_2977, proC
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 14 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: I222
Unit cell:
a: 52.98Å b: 68.45Å c: 149.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.231 0.262
Expression system: Escherichia coli

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