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PDBsum entry 1fea

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
1fea

 

 

 

 

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Contents
Protein chains
487 a.a. *
Ligands
FAD ×4
Waters ×362
* Residue conservation analysis
PDB id:
1fea
Name: Oxidoreductase
Title: Unliganded crithidia fasciculata trypanothione reductase at 2.2 angstrom resolution
Structure: Trypanothione reductase. Chain: a, b, c, d. Engineered: yes. Other_details: monoclinic crystal form, tetramer in the asymmetric unit
Source: Crithidia fasciculata. Organism_taxid: 5656. Gene: tr1. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: see strickland, et. Al. (1995) acta cryst. D51, 337- 341
Biol. unit: Homo-Dimer (from PDB file)
Resolution:
2.20Å     R-factor:   0.185    
Authors: C.Strickland,P.Karplus
Key ref: C.L.Strickland and p.a.karplus Crithidia fasciculata trypanothione reductase at 1.70 a resolution. To be published, .
Date:
12-Jul-95     Release date:   11-Jan-97    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P39040  (TYTR_CRIFA) -  Trypanothione reductase from Crithidia fasciculata
Seq:
Struc:
491 a.a.
487 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.1.8.1.12  - trypanothione-disulfide reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: trypanothione + NADP+ = trypanothione disulfide + NADPH + H+
trypanothione
+ NADP(+)
= trypanothione disulfide
+ NADPH
+ H(+)
      Cofactor: FAD
FAD
Bound ligand (Het Group name = FAD) corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

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