4RX3
A triple mutant in the omega-loop of TEM-1 beta-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis
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 | 17 |
Details | BINDING SITE FOR RESIDUE FLC A 301 |
Chain | Residue |
A | GLU28 |
A | ALA237 |
A | LYS288 |
A | HIS289 |
A | HOH403 |
A | HOH422 |
A | HOH432 |
A | HOH543 |
A | HOH609 |
A | MET69 |
A | GLY70 |
A | LYS73 |
A | TYR105 |
A | SER130 |
A | ASN132 |
A | TYR166 |
A | GLY236 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Acyl-ester intermediate |
Chain | Residue | Details |
A | GLY70 |
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 | GLY70 | 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 | TYR166 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | LYS234 | electrostatic stabiliser |
A | ALA237 | electrostatic stabiliser, hydrogen bond donor |