Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APBP_dimere3zg5A5 A: beta complex topologyX: Penicillin binding protein dimerisation domain (From Topology)H: Penicillin binding protein dimerisation domain (From Topology)T: Penicillin binding protein dimerisation domainF: PBP_dimerECOD (1.6)
ATranspeptidase_1ste3zg5A1 A: alpha complex topologyX: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology)H: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology)T: alpha-helical domain in beta-lactamase/transpeptidase-like proteinsF: Transpeptidase_1stECOD (1.6)
AMecA_Ne3zg5A7 A: a+b two layersX: Cystatin-likeH: NTF2-like (From Topology)T: NTF2-likeF: MecA_NECOD (1.6)
AEUF08385e3zg5A6 A: a+b two layersX: ClpS-likeH: Penicillin binding protein ClpS-like domain (From Topology)T: Penicillin binding protein ClpS-like domainF: EUF08385ECOD (1.6)
ATranspeptidase_2nde3zg5A3 A: a+b three layersX: Profilin-likeH: a+b domain in beta-lactamase/transpeptidase-like proteins (From Topology)T: a+b domain in beta-lactamase/transpeptidase-like proteinsF: Transpeptidase_2ndECOD (1.6)
BPBP_dimere3zg5B5 A: beta complex topologyX: Penicillin binding protein dimerisation domain (From Topology)H: Penicillin binding protein dimerisation domain (From Topology)T: Penicillin binding protein dimerisation domainF: PBP_dimerECOD (1.6)
BTranspeptidase_1ste3zg5B1 A: alpha complex topologyX: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology)H: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology)T: alpha-helical domain in beta-lactamase/transpeptidase-like proteinsF: Transpeptidase_1stECOD (1.6)
BMecA_Ne3zg5B7 A: a+b two layersX: Cystatin-likeH: NTF2-like (From Topology)T: NTF2-likeF: MecA_NECOD (1.6)
BEUF08385e3zg5B6 A: a+b two layersX: ClpS-likeH: Penicillin binding protein ClpS-like domain (From Topology)T: Penicillin binding protein ClpS-like domainF: EUF08385ECOD (1.6)
BTranspeptidase_2nde3zg5B3 A: a+b three layersX: Profilin-likeH: a+b domain in beta-lactamase/transpeptidase-like proteins (From Topology)T: a+b domain in beta-lactamase/transpeptidase-like proteinsF: Transpeptidase_2ndECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

AMR Gene: CARD Annotation CARD Database Homepage

ChainsAccessionShort NameDescriptionProvenance Source (Version)
A, B
ARO:3000617mecAA foreign PBP2a acquired by lateral gene transfer that is able to perform peptidoglycan synthesis in the presence of beta-lactams.CARD (3.3.0)

AMR Gene Family: CARD Annotation CARD Database Homepage

ChainsAccessionGene FamilyDrug Class Resistance MachanismProvenance Source (Version)
A, B
ARO:3001208methicillin resistant PBP2penamantibiotic target replacementCARD (3.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF03717Penicillin-binding Protein dimerisation domain (PBP_dimer)Penicillin-binding Protein dimerisation domainThis domain is found at the N terminus of Class B High Molecular Weight Penicillin-Binding Proteins. Its function has not been precisely defined, but is strongly implicated in PBP polymerisation. The domain forms a largely disordered 'sugar tongs' st ...This domain is found at the N terminus of Class B High Molecular Weight Penicillin-Binding Proteins. Its function has not been precisely defined, but is strongly implicated in PBP polymerisation. The domain forms a largely disordered 'sugar tongs' structure.
Domain
A, B
PF00905Penicillin binding protein transpeptidase domain (Transpeptidase)Penicillin binding protein transpeptidase domainThe active site serine (residue 337 in Swiss:P14677) is conserved in all members of this family.Domain
A, B
PF05223NTF2-like N-terminal transpeptidase domain (MecA_N)NTF2-like N-terminal transpeptidase domainThe structure of this domain from MecA is known [1] Swiss:Q53707 and is found to be similar to that found in NTF2 Pfam:PF02136. This domain seems unlikely to have an enzymatic function, and its role remains unknown.Domain

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
C, D
DAL RESIDAA0111 , AA0191

PSI-MOD :  meso-lanthionine MOD:00120 , D-alanine (Ala) MOD:00198 , D-alanine (Ser) MOD:00858 , D-alanine MOD:00862
C, D
FGA RESIDAA0111 , AA0191