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PDBsum entry 2y2b

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2y2b
Jmol
Contents
Protein chains
179 a.a.
Ligands
AH0
MHI
Metals
_ZN ×3
Waters ×556
PDB id:
2y2b
Name: Hydrolase
Title: Crystal structure of ampd in complex with reaction products
Structure: 1,6-anhydro-n-acetylmuramyl-l-alanine amidase amp chain: a, b, c. Synonym: ampd, n-acetylmuramoyl-l-alanine amidase. Engineered: yes
Source: Citrobacter freundii. Organism_taxid: 546. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.90Å     R-factor:   0.173     R-free:   0.223
Authors: C.Carrasco-Lopez,A.Rojas-Altuve,W.Zhang,D.Hesek,M.Lee,S.Barb I.Andre,N.Silva-Martin,M.Martinez-Ripoll,S.Mobashery,J.A.He
Key ref: 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: 21775432 DOI: 10.1074/jbc.M111.264366
Date:
14-Dec-10     Release date:   20-Jul-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P82974  (AMPD_CITFR) -  1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD
Seq:
Struc:
187 a.a.
179 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.5.1.28  - N-acetylmuramoyl-L-alanine amidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain bacterial cell-wall glycopeptides.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     peptidoglycan catabolic process   1 term 
  Biochemical function     hydrolase activity     3 terms  

 

 
DOI no: 10.1074/jbc.M111.264366 J Biol Chem 286:31714-31722 (2011)
PubMed id: 21775432  
 
 
Crystal structures of bacterial peptidoglycan amidase AmpD and an unprecedented activation mechanism.
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.
 
  ABSTRACT  
 
No abstract given.