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PDBsum entry 2y2c
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PDB id:
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Hydrolase
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Title:
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Crystal structure of ampd apoenzyme
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Structure:
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1,6-anhydro-n-acetylmuramyl-l-alanine amidase ampd. Chain: a, b, c. Synonym: ampd, n-acetylmuramoyl-l-alanine amidase. Engineered: yes. Other_details: ampd apoenzyme
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Source:
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Citrobacter freundii. Organism_taxid: 546. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.80Å
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R-factor:
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0.192
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R-free:
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0.246
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Authors:
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C.Carrasco-Lopez,A.Rojas-Altuve,W.Zhang,D.Hesek,M.Lee,S.Barbe, I.Andre,N.Silva-Martin,M.Martinez-Ripoll,S.Mobashery,J.A.Hermoso
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Key ref:
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C.Carrasco-López
et al.
(2011).
Crystal structures of bacterial peptidoglycan amidase AmpD and an unprecedented activation mechanism.
J Biol Chem,
286,
31714-31722.
PubMed id:
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Date:
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14-Dec-10
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Release date:
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20-Jul-11
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PROCHECK
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Headers
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References
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P82974
(AMPD_CITFR) -
1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD from Citrobacter freundii
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Seq: Struc:
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187 a.a.
179 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.3.5.1.28
- N-acetylmuramoyl-L-alanine amidase.
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Reaction:
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Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain bacterial cell-wall glycopeptides.
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J Biol Chem
286:31714-31722
(2011)
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PubMed id:
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Crystal structures of bacterial peptidoglycan amidase AmpD and an unprecedented activation mechanism.
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C.Carrasco-López,
A.Rojas-Altuve,
W.Zhang,
D.Hesek,
M.Lee,
S.Barbe,
I.André,
P.Ferrer,
N.Silva-Martin,
G.R.Castro,
M.Martínez-Ripoll,
S.Mobashery,
J.A.Hermoso.
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ABSTRACT
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');
}
}
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