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PDBsum entry 1gcu

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protein links
Oxidoreductase PDB id
1gcu
Jmol
Contents
Protein chain
292 a.a. *
Waters ×294
* Residue conservation analysis
PDB id:
1gcu
Name: Oxidoreductase
Title: Crystal structure of rat biliverdin reductase at 1.4 a
Structure: Biliverdin reductase a. Chain: a. Engineered: yes
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.40Å     R-factor:   0.219     R-free:   0.248
Authors: A.Kikuchi,S.Y.Park,Y.Shiro
Key ref:
D.Sun et al. (2000). Crystallization and preliminary X-ray diffraction analysis of a rat biliverdin reductase. Acta Crystallogr D Biol Crystallogr, 56, 1180-1182. PubMed id: 10957639 DOI: 10.1107/S0907444900008520
Date:
08-Aug-00     Release date:   08-Feb-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P46844  (BIEA_RAT) -  Biliverdin reductase A
Seq:
Struc:
295 a.a.
292 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.3.1.24  - Biliverdin reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Biliverdin metabolism
      Reaction: Bilirubin + NAD(P)(+) = biliverdin + NAD(P)H
Bilirubin
+ NAD(P)(+)
= biliverdin
+ NAD(P)H
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     oxidoreductase activity     4 terms  

 

 
    reference    
 
 
DOI no: 10.1107/S0907444900008520 Acta Crystallogr D Biol Crystallogr 56:1180-1182 (2000)
PubMed id: 10957639  
 
 
Crystallization and preliminary X-ray diffraction analysis of a rat biliverdin reductase.
D.Sun, M.Sato, T.Yoshida, H.Shimizu, H.Miyatake, S.Adachi, Y.Shiro, A.Kikuchi.
 
  ABSTRACT  
 
Biliverdin reductase (BVR) catalyzes the final step of haem degradation and converts biliverdin to bilirubin using NAD(P)H as an electron donor. This paper deals with the first crystallization and preliminary crystallographic study of recombinant rat BVR expressed in Escherichia coli. Crystals of BVR were obtained by the sitting-drop vapour-diffusion method. Using synchrotron radiation at station BL44B2 of SPring-8, Japan, BVR diffraction data were collected to 1.6 A resolution. Crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 58.89, b = 70.41, c = 87.76 A. The complete determination of the crystallographic structure is currently in progress using MAD (multiwavelength anomalous diffraction) data from an Ir-derivative crystal.
 
  Selected figure(s)  
 
Figure 2.
Figure 2 Bijvoet difference Patterson maps using the data collected at 1.1053 . Diffraction data in the resolution range 30-2 were used for calculation. Cross symbols correspond to Ir-Ir self-vectors. The position of the Ir atom is refined as (0.081, 0.139, 0.062) by vector-space refinement.
 
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2000, 56, 1180-1182) copyright 2000.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
16115896 T.Matsui, A.Nakajima, H.Fujii, K.M.Matera, C.T.Migita, T.Yoshida, and M.Ikeda-Saito (2005).
O(2)- and H(2)O(2)-dependent verdoheme degradation by heme oxygenase: reaction mechanisms and potential physiological roles of the dual pathway degradation.
  J Biol Chem, 280, 36833-36840.  
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