PDBe 2h63

X-ray diffraction
2.7Å resolution

Crystal Structure of Human Biliverdin Reductase A

Released:
Source organism: Homo sapiens
Entry authors: Kavanagh K, Elkins J, Ugochukwu E, Guo K, Pilka E, Lukacik P, Smee C, Papagrigoriou E, Bunkoczi G, Sundstrom M, Arrowsmith C, Weigelt J, Edwards A, von Delft F, Oppermann U, Structural Genomics Consortium (SGC)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Biliverdin reductase A Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 292 amino acids
Theoretical weight: 33.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53004 (Residues: 7-296; Coverage: 98%)
Gene names: BLVR, BLVRA, BVR
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 4 x NAP
No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 90.787Å b: 92.747Å c: 147.755Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.237 0.287
Expression system: Escherichia coli