1GCU

CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.248 
  • R-Value Work: 0.219 
  • R-Value Observed: 0.219 

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This is version 1.4 of the entry. See complete history. 


Literature

Crystal structure of rat biliverdin reductase.

Kikuchi, A., Park, S.Y., Miyatake, H., Sun, D., Sato, M., Yoshida, T., Shiro, Y.

(2001) Nat Struct Biol 8: 221-225

  • DOI: https://doi.org/10.1038/84955
  • Primary Citation of Related Structures:  
    1GCU

  • PubMed Abstract: 

    Biliverdin reductase (BVR) is a soluble cytoplasmic enzyme that catalyzes the conversion of biliverdin to bilirubin using NADH or NADPH as electron donor. Bilirubin is a significant biological antioxidant, but it is also neurotoxic and the cause of kernicterus. In this study, we have determined the crystal structure of rat BVR at 1.4 A resolution. The structure contains two domains: an N-terminal domain characteristic of a dinucleotide binding fold (Rossmann fold) and a C-terminal domain that is predominantly an antiparallel six-stranded beta-sheet. Based on this structure, we propose modes of binding for NAD(P)H and biliverdin, and a possible mechanism for the enzyme.

    • Organizational Affiliation: 

    RIKEN Harima Institute/SPring-8, Sayo, Hyogo 679-5148, Japan. kikuchi@spring8.or.jp


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
BILIVERDIN REDUCTASE A295Rattus norvegicusMutation(s): 0 
EC: 1.3.1.24
UniProt
Find proteins for P46844 (Rattus norvegicus)
Explore P46844 
Go to UniProtKB:  P46844
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP46844
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.248 
  • R-Value Work: 0.219 
  • R-Value Observed: 0.219 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 58.682α = 90
b = 70.487β = 90
c = 87.866γ = 90
Software Package:
Software NamePurpose
SHARPphasing
X-PLORrefinement
MOSFLMdata reduction
CCP4data scaling

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-02-08
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-10-11
    Changes: Data collection
  • Version 1.4: 2023-12-27
    Changes: Data collection, Database references