5NJ2
Crystal structure of BlaC from Mycobacterium tuberculosis bound to phosphate
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 |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 A 401 |
| Chain | Residue |
| A | SER70 |
| A | SER128 |
| A | LYS236 |
| A | THR237 |
| A | GLY238 |
| A | THR239 |
| A | HOH578 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 402 |
| Chain | Residue |
| A | LYS205 |
| A | HOH594 |
| A | PRO202 |
| A | ASP204 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 403 |
| Chain | Residue |
| A | GLY118 |
| A | GLN119 |
| A | ASP122 |
| A | TRP212 |
| A | HOH634 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue ACT A 404 |
| Chain | Residue |
| A | ARG173 |
| A | ASP241 |
| A | TYR273 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 B 401 |
| Chain | Residue |
| B | SER70 |
| B | SER128 |
| B | LYS236 |
| B | THR237 |
| B | GLY238 |
| B | THR239 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 B 402 |
| Chain | Residue |
| A | HIS300 |
| B | ARG173 |
| B | ASP241 |
| B | TYR273 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ACT B 403 |
| Chain | Residue |
| B | PRO202 |
| B | ASP204 |
| B | LYS205 |
| B | HOH608 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue ETE B 404 |
| Chain | Residue |
| A | HOH612 |
| B | THR210 |
| B | ALA214 |
| B | LYS232 |
| B | TRP252 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue AE4 B 405 |
| Chain | Residue |
| B | ALA31 |
| B | ALA57 |
| B | ILE58 |
| B | GLU59 |
| B | TYR60 |
| B | ARG61 |
| B | HOH509 |
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_FI1 |
| Number of Residues | 2 |
| 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 | 2 |
| 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 | 6 |
| 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 | 2 |
| 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 | 2 |
| 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 |
