7A6Z
Structure of P226G BlaC from Mycobacterium tuberculosis
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 | 9 |
| Details | binding site for residue GOL A 301 |
| Chain | Residue |
| A | GLN83 |
| A | ASN86 |
| A | ASP141 |
| A | ASP240 |
| A | TYR272 |
| A | ASP273 |
| A | GOL302 |
| A | HOH404 |
| A | HOH441 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 302 |
| Chain | Residue |
| A | ALA140 |
| A | ASP141 |
| A | GLU275 |
| A | PRO276 |
| A | GOL301 |
| A | HOH404 |
| A | HOH464 |
| A | HOH474 |
| A | HOH482 |
| A | HOH595 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | PRO107 |
| A | GLN110 |
| A | GLN111 |
| A | THR145 |
| A | ALA146 |
| A | THR149 |
| A | ARG161 |
| A | LEU162 |
| A | ASP163 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 304 |
| Chain | Residue |
| A | TYR97 |
| A | VAL113 |
| A | VAL291 |
| A | LEU292 |
| A | ALA293 |
| A | HOH406 |
| A | HOH412 |
| A | HOH593 |
| A | HOH603 |
| A | HOH615 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue GOL A 305 |
| Chain | Residue |
| A | MET211 |
| A | ALA212 |
| A | GLY217 |
| A | ALA218 |
| A | ARG222 |
| A | VAL231 |
| A | ILE232 |
| A | ASP233 |
| A | HOH413 |
| A | HOH419 |
| A | HOH478 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 306 |
| Chain | Residue |
| A | THR89 |
| A | HIS90 |
| A | LYS93 |
| A | ASP273 |
| A | HOH411 |
| A | HOH473 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 307 |
| Chain | Residue |
| A | ALA30 |
| A | ALA56 |
| A | ILE57 |
| A | GLU59 |
| A | TYR60 |
| A | HOH409 |
| A | HOH461 |
| A | HOH467 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 308 |
| Chain | Residue |
| A | ARG65 |
| A | PRO174 |
| A | GLY175 |
| A | ARG243 |
| A | HOH468 |
| A | HOH524 |
| A | HOH639 |
| A | HOH642 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 309 |
| Chain | Residue |
| A | ASP101 |
| A | ASN136 |
| A | GLU165 |
| A | HOH484 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue PO4 A 310 |
| Chain | Residue |
| A | SER70 |
| A | SER130 |
| A | LYS234 |
| A | THR235 |
| A | GLY236 |
| A | THR237 |
| A | HOH401 |
| A | HOH462 |
| A | HOH630 |
| A | HOH645 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 A 311 |
| Chain | Residue |
| A | LEU94 |
| A | GLY116 |
| A | GLN121 |
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 | PHE66-LEU81 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI2 |
| 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_FI3 |
| 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_FI4 |
| 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_FI5 |
| 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_FI6 |
| 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 |
