1JVJ
CRYSTAL STRUCTURE OF N132A MUTANT OF TEM-1 BETA-LACTAMASE IN COMPLEX WITH A N-FORMIMIDOYL-THIENAMYCINE
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 | 4 |
| Details | BINDING SITE FOR RESIDUE K A 501 |
| Chain | Residue |
| A | MET211 |
| A | ALA213 |
| A | ASP233 |
| A | HOH550 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 502 |
| Chain | Residue |
| A | LEU57 |
| A | GLU58 |
| A | ASN100 |
| A | HOH608 |
| A | HOH833 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 503 |
| Chain | Residue |
| A | ALA217 |
| A | LEU220 |
| A | LEU221 |
| A | ARG222 |
| A | ASP233 |
| A | ILE246 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 504 |
| Chain | Residue |
| A | TYR97 |
| A | LEU113 |
| A | HOH728 |
| A | HOH741 |
| A | HOH775 |
| A | HOH852 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K A 505 |
| Chain | Residue |
| A | ARG61 |
| A | PRO62 |
| A | GLU63 |
| A | HOH570 |
| A | HOH700 |
| A | HOH741 |
| A | HOH775 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE IM2 A 300 |
| Chain | Residue |
| A | MET69 |
| A | SER70 |
| A | LYS73 |
| A | TYR105 |
| A | SER130 |
| A | GLU166 |
| A | VAL216 |
| A | SER235 |
| A | GLY236 |
| A | ALA237 |
| A | ARG244 |
| A | HOH556 |
| A | HOH828 |
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":"Acyl-ester intermediate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| 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 |
