5g4k

X-ray diffraction
1.74Å resolution

Phloroglucinol reductase from Clostridium sp. apo-form

Released:
Source organism: Clostridium sp.
Primary publication:
Biocatalytic Properties and Structural Analysis of Phloroglucinol Reductases.
Angew Chem Int Ed Engl 55 15531-15534 (2016)
PMID: 27874239

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-165682 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
OXIDOREDUCTASE, SHORT CHAIN DEHYDROGENASE/REDUCTASE FAMILY PROTEIN Chain: A
Molecule details ›
Chain: A
Length: 286 amino acids
Theoretical weight: 31.15 KDa
Source organism: Clostridium sp.
Expression system: Escherichia coli BL21(DE3)
Structure domains: NAD(P)-binding Rossmann-like Domain
OXIDOREDUCTASE, SHORT CHAIN DEHYDROGENASE/REDUCTASE FAMILY PROTEIN Chain: B
Molecule details ›
Chain: B
Length: 286 amino acids
Theoretical weight: 31.12 KDa
Source organism: Clostridium sp.
Expression system: Escherichia coli BL21(DE3)
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21212
Unit cell:
a: 89.756Å b: 125.391Å c: 55.468Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.157 0.182
Expression system: Escherichia coli BL21(DE3)