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Go to PDB code:
Transferase
PDB id
1qgd
Contents
Protein chains
662 a.a.
*
Ligands
SO4
×2
TPP
×2
Metals
_CA
×2
Waters
×1065
*
Residue conservation analysis
PDB id:
1qgd
Links
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PROCOGNATE
ProSAT
EDS
Whatcheck
Name:
Transferase
Title:
Transketolase from escherichia coli
Structure:
Protein (transketolase). Chain: a, b. Engineered: yes
Source:
Escherichia coli. Organism_taxid: 562. Cellular_location: cytoplasm. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit:
Dimer (from
PQS
)
Resolution:
1.90Å
R-factor:
0.132
R-free:
0.176
Authors:
M.N.Isupov,J.A.Littlechild
Key ref:
M.N.Isupov et al. Crystal structure of escherichia coli transketolase.
To be published
,
Date:
23-Apr-99
Release date:
17-Jun-03
PROCHECK
Headers
References
Protein chains
?
P27302
(TKT1_ECOLI) - Transketolase 1
Seq:
Struc:
 
Seq:
Struc:
663 a.a.
662 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.2.2.1.1
- Transketolase.
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
Reaction:
Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate
Sedoheptulose 7-phosphate
+
D-glyceraldehyde 3-phosphate
=
D-ribose 5-phosphate
+
D-xylulose 5-phosphate
Cofactor:
Thiamine diphosphate
Thiamine diphosphate
Bound ligand (Het Group name =
TPP
) corresponds exactly
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
Gene Ontology (GO) functional annotation
Biological process
metabolic process
1 term
Biochemical function
catalytic activity
4 terms