THE REFINED CRYSTALLOGRAPHIC STRUCTURE OF A DD-PEPTIDASE PENICILLIN-TARGET ENZYME AT 1.6 A RESOLUTION
External Resource: Annotation
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
A | SCOP2B Superfamily | beta-lactamase/transpeptidase-like | 8034869 | 3001604 | SCOP2B (2022-06-29) |
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
A | Beta-lactamase_1st | e3pteA1 | A: alpha complex topology | X: 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 proteins | F: Beta-lactamase_1st | ECOD (1.6) |
A | Beta-lactamase_2nd | e3pteA2 | A: a+b three layers | X: Profilin-like | H: a+b domain in beta-lactamase/transpeptidase-like proteins (From Topology) | T: a+b domain in beta-lactamase/transpeptidase-like proteins | F: Beta-lactamase_2nd | ECOD (1.6) |
Chains | Accession | Name | Description | Comments | Source |
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| PF00144 | Beta-lactamase (Beta-lactamase) | Beta-lactamase | This family appears to be distantly related to Pfam:PF00905 and PF00768 D-alanyl-D-alanine carboxypeptidase. | Domain |
Chains | Polymer | Molecular Function | Biological Process | Cellular Component |
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| D-ALANYL-D-ALANINE CARBOXYPEPTIDASE TRANSPEPTIDASE | | | |