3SR3

Crystal structure of the w180a mutant of microcin immunity protein mccf from Bacillus anthracis shows the active site loop in the open conformation.


Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BPeptidase_S66_Ne3sr3B2 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: Class I glutamine amidotransferase-likeF: Peptidase_S66_NECOD (1.6)
BPeptidase_S66_Ce3sr3B1 A: a/b three-layered sandwichesX: The swivelling beta/beta/alpha domainsH: The swivelling beta/beta/alpha domain (From Topology)T: The swivelling beta/beta/alpha domainF: Peptidase_S66_CECOD (1.6)
APeptidase_S66_Ne3sr3A1 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: Class I glutamine amidotransferase-likeF: Peptidase_S66_NECOD (1.6)
APeptidase_S66_Ce3sr3A2 A: a/b three-layered sandwichesX: The swivelling beta/beta/alpha domainsH: The swivelling beta/beta/alpha domain (From Topology)T: The swivelling beta/beta/alpha domainF: Peptidase_S66_CECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF17676LD-carboxypeptidase C-terminal domain (Peptidase_S66C)LD-carboxypeptidase C-terminal domainMuramoyl-tetrapeptide carboxypeptidase hydrolyses a peptide bond between a di-basic amino acid and the C-terminal D-alanine in the tetrapeptide moiety in peptidoglycan. This cleaves the bond between an L- and a D-amino acid. ...Muramoyl-tetrapeptide carboxypeptidase hydrolyses a peptide bond between a di-basic amino acid and the C-terminal D-alanine in the tetrapeptide moiety in peptidoglycan. This cleaves the bond between an L- and a D-amino acid. The function of this activity is in murein recycling. This family also includes the microcin c7 self-immunity protein Swiss:Q47511. This family corresponds to Merops family S66.
Domain
A, B
PF02016LD-carboxypeptidase N-terminal domain (Peptidase_S66)LD-carboxypeptidase N-terminal domainMuramoyl-tetrapeptide carboxypeptidase hydrolyses a peptide bond between a di-basic amino acid and the C-terminal D-alanine in the tetrapeptide moiety in peptidoglycan. This cleaves the bond between an L- and a D-amino acid. The function of this acti ...Muramoyl-tetrapeptide carboxypeptidase hydrolyses a peptide bond between a di-basic amino acid and the C-terminal D-alanine in the tetrapeptide moiety in peptidoglycan. This cleaves the bond between an L- and a D-amino acid. The function of this activity is in murein recycling. This family also includes the microcin c7 self-immunity protein Swiss:Q47511. This family corresponds to Merops family S66.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage