3N7W
Crystal Structure of BlaC-E166A covalently bound with Amoxicillin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE AXL A 1 |
| Chain | Residue |
| A | CYS83 |
| A | PRO290 |
| A | PO4308 |
| A | HOH358 |
| A | HOH359 |
| A | HOH390 |
| A | HOH416 |
| A | HOH476 |
| A | SER84 |
| A | SER142 |
| A | ASN186 |
| A | GLU193 |
| A | THR251 |
| A | GLY252 |
| A | THR253 |
| A | GLY254 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 308 |
| Chain | Residue |
| A | AXL1 |
| A | ARG79 |
| A | ARG187 |
| A | GLU193 |
| A | ASP255 |
| A | TYR286 |
| A | HOH330 |
| A | HOH348 |
| A | HOH359 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 309 |
| Chain | Residue |
| A | HOH16 |
| A | ARG75 |
| A | GLU78 |
| A | GLU184 |
| A | HOH316 |
| A | HOH486 |
Functional Information from PROSITE/UniProt
| site_id | PS00146 |
| Number of Residues | 16 |
| Details | BETA_LACTAMASE_A Beta-lactamase class-A active site. FaFCSTfKaplVAAVL |
| Chain | Residue | Details |
| A | PHE80-LEU95 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PubMed","id":"19251630","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20353175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20961112","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"20353175","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20961112","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19251630","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20353175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20961112","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Increases nucleophilicity of active site Ser","evidences":[{"source":"PubMed","id":"20353175","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20961112","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Functions as a gatekeeper residue that regulates substrate accessibility to the enzyme active site","evidences":[{"source":"PubMed","id":"24023821","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
