3NPF

Crystal structure of a putative dipeptidyl-peptidase VI (BACOVA_00612) from Bacteroides ovatus at 1.72 A resolution


Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF08239e3npfA3 A: beta barrelsX: SH3H: SH3T: SH3F: PF08239ECOD (1.6)
APF18348e3npfA2 A: beta barrelsX: SH3H: SH3T: SH3F: PF18348ECOD (1.6)
APF00877e3npfA1 A: a+b complex topologyX: Cysteine proteinases-likeH: Cysteine proteinases (From Topology)T: Cysteine proteinasesF: PF00877ECOD (1.6)
BPF08239e3npfB7 A: beta barrelsX: SH3H: SH3T: SH3F: PF08239ECOD (1.6)
BPF18348e3npfB6 A: beta barrelsX: SH3H: SH3T: SH3F: PF18348ECOD (1.6)
BPF00877e3npfB3 A: a+b complex topologyX: Cysteine proteinases-likeH: Cysteine proteinases (From Topology)T: Cysteine proteinasesF: PF00877ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF00877NlpC/P60 family (NLPC_P60)NlpC/P60 family- Family
A, B
PF18348Bacterial dipeptidyl-peptidase Sh3 domain (SH3_16)Bacterial dipeptidyl-peptidase Sh3 domainThis is the first of two N-terminal bacterial SH3 (SH3b) domains found in bacterial dipeptidyl-peptidases VI such as gamma-D-glutamyl-L-diamino acid endopeptidases. The first SH3b domain plays an important role in defining substrate specificity by co ...This is the first of two N-terminal bacterial SH3 (SH3b) domains found in bacterial dipeptidyl-peptidases VI such as gamma-D-glutamyl-L-diamino acid endopeptidases. The first SH3b domain plays an important role in defining substrate specificity by contributing to the formation of the active site, such that only murein peptides with a free N-terminal alanine are allowed [1].
Domain