4RX2
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 |
| B | 0005515 | molecular_function | protein binding |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| B | 0046677 | biological_process | response to antibiotic |
| C | 0005515 | molecular_function | protein binding |
| C | 0008800 | molecular_function | beta-lactamase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0017001 | biological_process | antibiotic catabolic process |
| C | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| C | 0046677 | biological_process | response to antibiotic |
| D | 0005515 | molecular_function | protein binding |
| D | 0008800 | molecular_function | beta-lactamase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0017001 | biological_process | antibiotic catabolic process |
| D | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| D | 0046677 | biological_process | response to antibiotic |
| E | 0005515 | molecular_function | protein binding |
| E | 0008800 | molecular_function | beta-lactamase activity |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0017001 | biological_process | antibiotic catabolic process |
| E | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| E | 0046677 | biological_process | response to antibiotic |
| F | 0005515 | molecular_function | protein binding |
| F | 0008800 | molecular_function | beta-lactamase activity |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0017001 | biological_process | antibiotic catabolic process |
| F | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| F | 0046677 | biological_process | response to antibiotic |
| G | 0005515 | molecular_function | protein binding |
| G | 0008800 | molecular_function | beta-lactamase activity |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0017001 | biological_process | antibiotic catabolic process |
| G | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| G | 0046677 | biological_process | response to antibiotic |
| H | 0005515 | molecular_function | protein binding |
| H | 0008800 | molecular_function | beta-lactamase activity |
| H | 0016787 | molecular_function | hydrolase activity |
| H | 0017001 | biological_process | antibiotic catabolic process |
| H | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| H | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 A 301 |
| Chain | Residue |
| A | SER70 |
| A | HOH458 |
| A | HOH477 |
| A | SER130 |
| A | VAL216 |
| A | LYS234 |
| A | SER235 |
| A | GLY236 |
| A | ARG244 |
| A | HOH421 |
| A | HOH453 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 301 |
| Chain | Residue |
| B | SER70 |
| B | SER130 |
| B | VAL216 |
| B | LYS234 |
| B | SER235 |
| B | GLY236 |
| B | ALA237 |
| B | ARG244 |
| B | HOH461 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 C 301 |
| Chain | Residue |
| C | SER130 |
| C | LYS234 |
| C | SER235 |
| C | GLY236 |
| C | ALA237 |
| C | ARG244 |
| C | HOH424 |
| C | HOH497 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 D 301 |
| Chain | Residue |
| D | SER70 |
| D | SER130 |
| D | VAL216 |
| D | LYS234 |
| D | SER235 |
| D | GLY236 |
| D | ARG244 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 E 301 |
| Chain | Residue |
| E | SER70 |
| E | SER130 |
| E | LYS234 |
| E | SER235 |
| E | GLY236 |
| E | ALA237 |
| E | ARG244 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 F 301 |
| Chain | Residue |
| F | SER70 |
| F | SER130 |
| F | LYS234 |
| F | SER235 |
| F | GLY236 |
| F | ALA237 |
| F | ARG244 |
| F | HOH416 |
| F | HOH434 |
| F | HOH472 |
| F | HOH488 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 G 301 |
| Chain | Residue |
| G | SER70 |
| G | SER130 |
| G | LYS234 |
| G | SER235 |
| G | GLY236 |
| G | ARG244 |
| G | HOH456 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 H 301 |
| Chain | Residue |
| H | SER70 |
| H | SER130 |
| H | VAL216 |
| H | LYS234 |
| H | SER235 |
| H | GLY236 |
| H | ALA237 |
| H | ARG244 |
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 | 8 |
| Details | ACT_SITE: Acyl-ester intermediate |
| Chain | Residue | Details |
| A | SER70 | |
| B | SER70 | |
| C | SER70 | |
| D | SER70 | |
| E | SER70 | |
| F | SER70 | |
| G | SER70 | |
| H | SER70 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | GLU168 | |
| B | GLU168 | |
| C | GLU168 | |
| D | GLU168 | |
| E | GLU168 | |
| F | GLU168 | |
| G | GLU168 | |
| H | GLU168 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS234 | |
| B | LYS234 | |
| C | LYS234 | |
| D | LYS234 | |
| E | LYS234 | |
| F | LYS234 | |
| G | LYS234 | |
| H | 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 | 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 |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 2 |
| Chain | Residue | Details |
| B | SER70 | electrostatic stabiliser |
| B | LYS73 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | SER130 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | TYR166 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | LYS234 | electrostatic stabiliser |
| B | ALA237 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 2 |
| Chain | Residue | Details |
| C | SER70 | electrostatic stabiliser |
| C | LYS73 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | SER130 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | TYR166 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | LYS234 | electrostatic stabiliser |
| C | ALA237 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 2 |
| Chain | Residue | Details |
| D | SER70 | electrostatic stabiliser |
| D | LYS73 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | SER130 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | TYR166 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | LYS234 | electrostatic stabiliser |
| D | ALA237 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA5 |
| Number of Residues | 6 |
| Details | M-CSA 2 |
| Chain | Residue | Details |
| E | SER70 | electrostatic stabiliser |
| E | LYS73 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| E | SER130 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| E | TYR166 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| E | LYS234 | electrostatic stabiliser |
| E | ALA237 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA6 |
| Number of Residues | 6 |
| Details | M-CSA 2 |
| Chain | Residue | Details |
| F | SER70 | electrostatic stabiliser |
| F | LYS73 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| F | SER130 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| F | TYR166 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| F | LYS234 | electrostatic stabiliser |
| F | ALA237 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA7 |
| Number of Residues | 6 |
| Details | M-CSA 2 |
| Chain | Residue | Details |
| G | SER70 | electrostatic stabiliser |
| G | LYS73 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| G | SER130 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| G | TYR166 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| G | LYS234 | electrostatic stabiliser |
| G | ALA237 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA8 |
| Number of Residues | 6 |
| Details | M-CSA 2 |
| Chain | Residue | Details |
| H | SER70 | electrostatic stabiliser |
| H | LYS73 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| H | SER130 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| H | TYR166 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| H | LYS234 | electrostatic stabiliser |
| H | ALA237 | electrostatic stabiliser, hydrogen bond donor |
