1JVJ
CRYSTAL STRUCTURE OF N132A MUTANT OF TEM-1 BETA-LACTAMASE IN COMPLEX WITH A N-FORMIMIDOYL-THIENAMYCINE
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 | 4 |
Details | BINDING SITE FOR RESIDUE K A 501 |
Chain | Residue |
A | MET211 |
A | ALA213 |
A | ASP233 |
A | HOH550 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K A 502 |
Chain | Residue |
A | LEU57 |
A | GLU58 |
A | ASN100 |
A | HOH608 |
A | HOH833 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K A 503 |
Chain | Residue |
A | ALA217 |
A | LEU220 |
A | LEU221 |
A | ARG222 |
A | ASP233 |
A | ILE246 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K A 504 |
Chain | Residue |
A | TYR97 |
A | LEU113 |
A | HOH728 |
A | HOH741 |
A | HOH775 |
A | HOH852 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE K A 505 |
Chain | Residue |
A | ARG61 |
A | PRO62 |
A | GLU63 |
A | HOH570 |
A | HOH700 |
A | HOH741 |
A | HOH775 |
site_id | AC6 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE IM2 A 300 |
Chain | Residue |
A | MET69 |
A | SER70 |
A | LYS73 |
A | TYR105 |
A | SER130 |
A | GLU166 |
A | VAL216 |
A | SER235 |
A | GLY236 |
A | ALA237 |
A | ARG244 |
A | HOH556 |
A | HOH828 |
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 | 1 |
Details | ACT_SITE: Acyl-ester intermediate |
Chain | Residue | Details |
A | SER70 |
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 | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1btl |
Chain | Residue | Details |
A | GLU166 | |
A | LYS73 | |
A | SER130 | |
A | SER70 |
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 |