1JWV
Crystal structure of G238A mutant of TEM-1 beta-lactamase in complex with a boronic acid inhibitor (sefb4)
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 | 6 |
| Details | BINDING SITE FOR RESIDUE K A 1 |
| Chain | Residue |
| A | TYR97 |
| A | LEU113 |
| A | HOH535 |
| A | HOH565 |
| A | HOH573 |
| A | HOH574 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 2 |
| Chain | Residue |
| A | HOH402 |
| A | HOH425 |
| A | HOH542 |
| A | LEU57 |
| A | GLU58 |
| A | ASN100 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 3 |
| Chain | Residue |
| A | LEU57 |
| A | GLU58 |
| A | HOH314 |
| A | HOH402 |
| A | HOH464 |
| A | HOH594 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 4 |
| Chain | Residue |
| A | K5 |
| A | LYS111 |
| A | LEU113 |
| A | THR114 |
| A | HOH322 |
| A | HOH338 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K A 5 |
| Chain | Residue |
| A | K4 |
| A | HOH301 |
| A | HOH353 |
| A | HOH388 |
| A | HOH391 |
| A | HOH415 |
| A | HOH666 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE CB4 A 300 |
| Chain | Residue |
| A | MET69 |
| A | SER70 |
| A | TYR105 |
| A | SER130 |
| A | ASN132 |
| A | GLY236 |
| A | ALA237 |
| A | ALA238 |
| A | GLU240 |
| A | HOH432 |
| A | HOH486 |
| A | HOH526 |
| A | HOH616 |
| A | HOH628 |
| A | HOH663 |
| A | HOH664 |
| A | HOH686 |
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 | ACT_SITE: Acyl-ester intermediate |
| Chain | Residue | Details |
| A | SER70 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | GLU168 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS234 |
Catalytic Information from CSA
| 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 |
