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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
1qgd
Jmol
Contents
Protein chains
662 a.a. *
Ligands
SO4 ×2
TPP ×2
Metals
_CA ×2
Waters ×1065
* Residue conservation analysis
PDB id:
1qgd
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
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
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 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     catalytic activity     4 terms