7TI1
Structure of AmpC bound to RPX-7063 at 2.0A
Functional Information from GO Data
Functional Information from PROSITE/UniProt
site_id | PS00336 |
Number of Residues | 8 |
Details | BETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSISK |
Chain | Residue | Details |
A | PHE80-LYS87 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active site: {"description":"Acyl-ester intermediate"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 257 |
Chain | Residue | Details |
A | SER84 | electrostatic stabiliser, hydrogen bond donor |
A | LYS87 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
A | TYR170 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLU292 | electrostatic stabiliser, hydrogen bond acceptor |
A | LYS335 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
A | SER338 | electrostatic stabiliser, hydrogen bond donor |