1GCE
STRUCTURE OF THE BETA-LACTAMASE OF ENTEROBACTER CLOACAE GC1
Functional Information from GO Data
Functional Information from PDB Data
site_id | ASA |
Number of Residues | 4 |
Details | CATALYTIC SITE |
Chain | Residue |
A | SER64 |
A | LYS67 |
A | TYR150 |
A | LYS318 |
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 | PHE60-LYS67 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Acyl-ester intermediate |
Chain | Residue | Details |
A | SER64 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | TYR150 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS318 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 257 |
Chain | Residue | Details |
A | SER64 | electrostatic stabiliser, hydrogen bond donor |
A | LYS67 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
A | TYR150 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLU275 | electrostatic stabiliser, hydrogen bond acceptor |
A | LYS318 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
A | SER321 | electrostatic stabiliser, hydrogen bond donor |