4MEZ
Crystal structure of M68L/M69T double mutant TEM-1
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 302 |
Chain | Residue |
A | PRO174 |
A | ARG241 |
A | HOH416 |
A | HOH435 |
B | ARG178 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 303 |
Chain | Residue |
A | HOH462 |
A | PRO252 |
A | SER258 |
A | ARG259 |
A | TRP290 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 304 |
Chain | Residue |
A | GLN90 |
A | LEU91 |
A | GLY92 |
A | ARG120 |
A | HOH493 |
A | HOH560 |
B | GLN90 |
B | LEU91 |
B | GLY92 |
B | ARG120 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 301 |
Chain | Residue |
B | ARG93 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 302 |
Chain | Residue |
A | HOH541 |
B | SER258 |
B | ARG259 |
B | TRP290 |
B | HOH548 |
Functional Information from PROSITE/UniProt
site_id | PS00146 |
Number of Residues | 16 |
Details | BETA_LACTAMASE_A Beta-lactamase class-A active site. FpLTSTfKvllCGAVL |
Chain | Residue | Details |
A | PHE66-LEU81 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Acyl-ester intermediate |
Chain | Residue | Details |
A | SER70 | |
B | SER70 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | GLU168 | |
B | GLU168 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS234 | |
B | 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 |