Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008800 | molecular_function | beta-lactamase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0017001 | biological_process | antibiotic catabolic process |
A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
A | 0042597 | cellular_component | periplasmic space |
A | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue KJK A 401 |
Chain | Residue |
A | SER64 |
A | GLY320 |
A | ASN346 |
A | HOH524 |
A | HOH711 |
A | GLN120 |
A | TYR150 |
A | ASN152 |
A | ASN289 |
A | LYS315 |
A | THR316 |
A | ALA318 |
A | THR319 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue MES A 402 |
Chain | Residue |
A | GLN22 |
A | GLN23 |
A | LYS24 |
A | TYR40 |
A | THR42 |
A | GLN56 |
A | HOH506 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue PEG A 403 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO A 404 |
Chain | Residue |
A | PRO5 |
A | LEU241 |
A | GLN249 |
A | HOH548 |
A | HOH671 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue EDO A 405 |
Chain | Residue |
A | GLY36 |
A | LYS37 |
A | GLN235 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue EDO A 406 |
Chain | Residue |
A | LYS50 |
A | GLY206 |
A | LYS207 |
A | ALA208 |
site_id | AC7 |
Number of Residues | 11 |
Details | binding site for residue K9K A 407 |
Chain | Residue |
A | THR97 |
A | GLN136 |
A | ASN137 |
A | PRO140 |
A | ALA141 |
A | TRP142 |
A | HOH509 |
A | HOH513 |
A | HOH593 |
A | HOH597 |
A | HOH658 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue ZN A 408 |
Chain | Residue |
A | HIS13 |
A | HIS13 |
A | HIS13 |
A | CL410 |
A | CL410 |
A | CL410 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue ZN A 409 |
Chain | Residue |
A | THR17 |
A | GLU21 |
A | HOH775 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue CL A 410 |
Chain | Residue |
A | HIS13 |
A | HIS13 |
A | HIS13 |
A | ZN408 |
A | ZN408 |
A | ZN408 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue CL A 411 |
Chain | Residue |
A | GLY320 |
A | HOH727 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue CL A 412 |
Chain | Residue |
A | GLU171 |
A | GLN175 |
A | ILE189 |
A | ASN190 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue NA A 413 |
Chain | Residue |
A | ASP217 |
A | HOH521 |
A | HOH646 |
A | HOH742 |
Functional Information from PROSITE/UniProt
site_id | PS00336 |
Number of Residues | 8 |
Details | BETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK |
Chain | Residue | Details |
A | PHE60-LYS67 | |
Functional Information from SwissProt/UniProt
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: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | LYS315 | |