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PDBsum entry 4b9b

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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
4b9b

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
(+ 2 more) 436 a.a.
Ligands
PLP ×8
GOL ×10
Metals
_CL ×8
_CA ×4
Waters ×4574
PDB id:
4b9b
Name: Transferase
Title: The structure of the omega aminotransferase from pseudomonas aeruginosa
Structure: Beta-alanine-pyruvate transaminase. Chain: a, b, c, d, e, f, g, h. Synonym: aminotransferase. Engineered: yes
Source: Pseudomonas aeruginosa. Organism_taxid: 287. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
1.64Å     R-factor:   0.177     R-free:   0.219
Authors: C.Sayer,M.N.Isupov,A.Westlake,J.A.Littlechild
Key ref: C.Sayer et al. (2013). Structural studies of Pseudomonas and Chromobacterium ω-aminotransferases provide insights into their differing substrate specificity. Acta Crystallogr D Biol Crystallogr, 69, 564-576. PubMed id: 23519665 DOI: 10.1107/S0907444912051670
Date:
03-Sep-12     Release date:   27-Mar-13    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9I700  (BAUA_PSEAE) -  Beta-alanine--pyruvate aminotransferase from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Seq:
Struc:
448 a.a.
436 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.6.1.18  - beta-alanine--pyruvate transaminase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 3-oxopropanoate + L-alanine = beta-alanine + pyruvate
3-oxopropanoate
Bound ligand (Het Group name = GOL)
matches with 71.43% similarity
+ L-alanine
= beta-alanine
+ pyruvate
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Bound ligand (Het Group name = PLP) corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1107/S0907444912051670 Acta Crystallogr D Biol Crystallogr 69:564-576 (2013)
PubMed id: 23519665  
 
 
Structural studies of Pseudomonas and Chromobacterium ω-aminotransferases provide insights into their differing substrate specificity.
C.Sayer, M.N.Isupov, A.Westlake, J.A.Littlechild.
 
  ABSTRACT  
 
No abstract given.

 

 

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