5I63
Crystal structure of TEM1 beta-lactamase mutant I263N in the presence of 1.2 MPa xenon
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue XE A 301 |
| Chain | Residue |
| A | LEU40 |
| A | THR265 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue XE A 302 |
| Chain | Residue |
| A | ASN263 |
| A | ILE279 |
| A | ILE282 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue XE B 301 |
| Chain | Residue |
| B | ASN263 |
| B | ILE279 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue XE B 302 |
| Chain | Residue |
| B | LEU221 |
| B | ILE279 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue XE C 302 |
| Chain | Residue |
| C | LEU221 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue XE D 301 |
| Chain | Residue |
| D | ASN263 |
| D | ILE279 |
| D | ILE282 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue XE D 302 |
| Chain | Residue |
| D | LEU221 |
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 | 4 |
| Details | ACT_SITE: Acyl-ester intermediate |
| Chain | Residue | Details |
| A | SER70 | |
| B | SER70 | |
| C | SER70 | |
| D | SER70 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | GLU168 | |
| B | GLU168 | |
| C | GLU168 | |
| D | GLU168 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS234 | |
| B | LYS234 | |
| C | LYS234 | |
| D | 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 |
| 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 | GLU166 | 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 | GLU166 | 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 | GLU166 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | LYS234 | electrostatic stabiliser |
| D | ALA237 | electrostatic stabiliser, hydrogen bond donor |
