6B2N
Crystal structure of TEM-1 beta-lactamase mutant M182N
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 | 5 |
Details | binding site for residue SO4 B 301 |
Chain | Residue |
A | LEU201 |
A | ARG204 |
B | ARG65 |
B | ARG161 |
B | GLU177 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue SO4 C 301 |
Chain | Residue |
C | THR200 |
C | LEU201 |
C | ARG204 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue SO4 D 301 |
Chain | Residue |
D | ARG240 |
D | ARG243 |
D | HOH408 |
D | GLU171 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue SO4 D 302 |
Chain | Residue |
D | THR200 |
D | LEU201 |
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 |