› 1lc3

X-ray diffraction
1.5Å resolution

Crystal Structure of a Biliverdin Reductase Enzyme-Cofactor Complex

Released:
DOI: 10.2210/pdb1lc3/pdb
PDB entry 1lc3 coloured by chain, front view.
PDB entry 1lc3 coloured by chain, side view.
PDB entry 1lc3 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex.
Whitby FG, Phillips JD, Hill CP, McCoubrey W, Maines MD
J Mol Biol 319 1199-210 (2002)
PMID: 12079357

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155517 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Biliverdin reductase A Chain: A
Molecule details ›
Chain: A
Length: 294 amino acids
Theoretical weight: 33.39 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P46844 (Residues: 8-295; Coverage: 98%)
Gene names: Blvr, Blvra
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
1 bound ligand:
Ligand PO4 3 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P212121
Unit cell:
a: 51.78Å b: 76.14Å c: 75.01Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.234
Expression system: Escherichia coli

Quick links

Citations

7 review citations

New insights into biliverdin reductase functions: linking heme metabolism to cell signaling.
Maines MD. (2005)
6 more

4 mentions without citation

Endoplasmic reticulum: a focal point of Zika virus infection.
Mohd Ropidi et al. (2020)
3 more