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PDBsum entry 1fea
Go to PDB code:
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
Links
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CATH
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CSA
PROCOGNATE
ProSAT
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
Headers
References
Protein chains
?
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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