1BT5
CRYSTAL STRUCTURE OF THE IMIPENEM INHIBITED TEM-1 BETA-LACTAMASE FROM ESCHERICHIA COLI
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 | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 351 |
| Chain | Residue |
| A | SER258 |
| A | ARG259 |
| A | TRP290 |
| A | HOH412 |
| A | HOH568 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 352 |
| Chain | Residue |
| A | HOH569 |
| A | THR271 |
| A | ASP273 |
| A | GLU274 |
| A | ARG277 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 353 |
| Chain | Residue |
| A | ARG43 |
| A | PRO174 |
| A | ASN175 |
| A | HOH422 |
| A | HOH642 |
| A | HOH689 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 A 354 |
| Chain | Residue |
| A | ARG161 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 355 |
| Chain | Residue |
| A | HIS153 |
| A | HIS158 |
| A | TRP229 |
| A | HOH409 |
| A | HOH610 |
| A | HOH659 |
| A | HOH662 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 356 |
| Chain | Residue |
| A | ARG178 |
| A | ALA202 |
| A | HOH483 |
| A | HOH489 |
| A | HOH496 |
| A | HOH630 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 357 |
| Chain | Residue |
| A | GLN90 |
| A | LEU91 |
| A | GLY92 |
| A | ARG120 |
| A | HOH478 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 358 |
| Chain | Residue |
| A | ARG94 |
| A | HIS96 |
| A | HOH606 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE IM2 A 350 |
| Chain | Residue |
| A | SER70 |
| A | SER130 |
| A | ASN132 |
| A | GLU166 |
| A | ASN170 |
| A | SER235 |
| A | GLY236 |
| A | ALA237 |
| A | GLY238 |
| A | ARG244 |
| A | MET272 |
| A | HOH390 |
| A | HOH521 |
| A | HOH590 |
| A | HOH654 |
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 |
