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PDBsum entry 4b9b
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PDB id:
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Transferase
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Title:
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The structure of the omega aminotransferase from pseudomonas aeruginosa
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Structure:
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Beta-alanine-pyruvate transaminase. Chain: a, b, c, d, e, f, g, h. Synonym: aminotransferase. Engineered: yes
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Source:
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Pseudomonas aeruginosa. Organism_taxid: 287. Expressed in: escherichia coli. Expression_system_taxid: 511693.
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Resolution:
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1.64Å
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R-factor:
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0.177
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R-free:
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0.219
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Authors:
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C.Sayer,M.N.Isupov,A.Westlake,J.A.Littlechild
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Key ref:
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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:
DOI:
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Date:
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03-Sep-12
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Release date:
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27-Mar-13
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PROCHECK
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Headers
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References
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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)
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Seq: Struc:
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448 a.a.
436 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.2.6.1.18
- beta-alanine--pyruvate transaminase.
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Reaction:
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3-oxopropanoate + L-alanine = beta-alanine + pyruvate
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3-oxopropanoate
Bound ligand (Het Group name = )
matches with 71.43% similarity
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L-alanine
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=
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beta-alanine
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+
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pyruvate
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Cofactor:
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Pyridoxal 5'-phosphate
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Pyridoxal 5'-phosphate
Bound ligand (Het Group name =
PLP)
corresponds exactly
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Acta Crystallogr D Biol Crystallogr
69:564-576
(2013)
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PubMed id:
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Structural studies of Pseudomonas and Chromobacterium ω-aminotransferases provide insights into their differing substrate specificity.
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C.Sayer,
M.N.Isupov,
A.Westlake,
J.A.Littlechild.
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ABSTRACT
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');
}
}
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