1PZP
TEM-1 Beta-Lactamase in Complex with a Novel, Core-Disrupting, Allosteric Inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| 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 | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FTA A 300 |
| Chain | Residue |
| A | MET155 |
| A | ARG191 |
| A | LYS192 |
| A | ALA224 |
| A | ILE263 |
| A | ALA280 |
| A | GLY283 |
| A | ALA284 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE FTA A 301 |
| Chain | Residue |
| A | LEU30 |
| A | LYS34 |
| A | PHE60 |
| A | ARG61 |
| A | ARG93 |
| A | HIS96 |
| A | ASP101 |
| A | ASN136 |
| A | LEU137 |
| A | THR140 |
| A | THR141 |
| A | TRP165 |
| A | HOH394 |
| A | HOH476 |
| A | HOH484 |
| A | PRO27 |
Functional Information from PROSITE/UniProt
| site_id | PS00146 |
| Number of Residues | 16 |
| Details | BETA_LACTAMASE_A Beta-lactamase class-A active site. FpMMSTfKvllCGAVL |
| Chain | Residue | Details |
| A | PHE66-LEU81 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile; acyl-ester intermediate","evidences":[{"source":"PubMed","id":"9485412","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"9485412","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"9485412","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| A | GLU166 | |
| A | LYS73 | |
| A | SER130 | |
| A | SER70 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 2 |
| Chain | Residue | Details |
| A | SER70 | electrostatic stabiliser |
| A | LYS73 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | SER130 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU166 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | LYS234 | electrostatic stabiliser |
| A | ALA237 | electrostatic stabiliser, hydrogen bond donor |
