Your browser does not support inline frames or is currently configured not to display inline frames. Content can be viewed at actual source page: inc/head.html
PDBsum entry 3ajh
Go to PDB code:
Oxidoreductase
PDB id
3ajh
Loading ...
Contents
Protein chains
240 a.a.
Ligands
BL3
×2
Waters
×134
PDB id:
3ajh
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
ProSAT
Name:
Oxidoreductase
Title:
Crystal structure of pcya v225d-biliverdin xiii alpha complex
Structure:
Phycocyanobilin:ferredoxin oxidoreductase. Chain: a, b. Fragment: v225d. Engineered: yes
Source:
Synechocystis. Organism_taxid: 1148. Strain: pcc 6803. Gene: pcya, slr0116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.25Å
R-factor:
0.251
R-free:
0.289
Authors:
K.Wada,Y.Hagiwara,K.Fukuyama
Key ref:
K.Wada et al. (2010). One residue substitution in PcyA leads to unexpected changes in tetrapyrrole substrate binding.
Biochem Biophys Res Commun
,
402
, 373-377.
PubMed id:
20946883
Date:
05-Jun-10
Release date:
16-Mar-11
PROCHECK
Headers
References
Protein chains
?
Q55891
(PCYA_SYNY3) - Phycocyanobilin:ferredoxin oxidoreductase from Synechocystis sp. (strain PCC 6803 / Kazusa)
Seq:
Struc:
248 a.a.
240 a.a.
*
Key:
PfamA domain
Secondary structure
CATH domain
*
PDB and UniProt seqs differ at 1 residue position (black cross)
Enzyme reactions
Enzyme class:
E.C.1.3.7.5
- phycocyanobilin:ferredoxin oxidoreductase.
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
Pathway:
Biliverdin metabolism
Reaction:
(2R,3Z)-phycocyanobilin + 4 oxidized [2Fe-2S]-[ferredoxin] = biliverdin IXalpha + 4 reduced [2Fe-2S]-[ferredoxin] + 4 H
+
(3Z)-phycocyanobilin
+
4 × oxidized ferredoxin
=
biliverdin IX-alpha
+
4 × reduced ferredoxin
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
Added reference
Biochem Biophys Res Commun
402
:373-377 (2010)
PubMed id:
20946883
One residue substitution in PcyA leads to unexpected changes in tetrapyrrole substrate binding.
K.Wada,
Y.Hagiwara,
Y.Yutani,
K.Fukuyama.
ABSTRACT
No abstract given.
'); } }