PDBe 1gcu

X-ray diffraction
1.4Å resolution

CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A

Released:
Source organism: Rattus norvegicus
Primary publication:
Crystal structure of rat biliverdin reductase.
Nat. Struct. Biol. 8 221-5 (2001)
PMID: 11224565

Function and Biology Details

Reaction catalysed:
Bilirubin + NAD(P)(+) = biliverdin + NAD(P)H. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Biliverdin reductase A Chain: A
Molecule details ›
Chain: A
Length: 295 amino acids
Theoretical weight: 33.61 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P46844 (Residues: 1-295; Coverage: 100%)
Gene names: Blvr, Blvra
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P212121
Unit cell:
a: 58.682Å b: 70.487Å c: 87.866Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.219 0.248
Expression system: Escherichia coli