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 | 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 CL A 301 |
Chain | Residue |
A | PRO201 |
A | ALA202 |
A | PRO243 |
A | LYS244 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue CIT A 302 |
Chain | Residue |
A | HOH472 |
A | HOH484 |
A | HOH485 |
A | HOH510 |
A | HOH589 |
A | LYS73 |
A | SER75 |
A | ARG128 |
A | LYS172 |
A | HOH419 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | SER75 |
A | ARG166 |
A | LEU170 |
A | HOH436 |
A | HOH437 |
A | HOH447 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue EDO A 304 |
Chain | Residue |
A | ALA54 |
A | HOH405 |
A | HOH418 |
A | HOH433 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue EDO A 305 |
Chain | Residue |
A | LEU66 |
A | SER177 |
A | GLN178 |
A | GLN181 |
A | HOH404 |
A | HOH430 |
A | HOH438 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO A 306 |
Chain | Residue |
A | GLU13 |
A | GLY18 |
A | ARG19 |
A | ARG36 |
A | HOH409 |
A | HOH634 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue EDO A 307 |
Chain | Residue |
A | ILE25 |
A | ASN30 |
A | GLN32 |
A | SER122 |
A | GLN163 |
A | ARG166 |
A | HOH418 |
A | HOH433 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue EDO A 308 |
Chain | Residue |
A | LEU34 |
A | ARG36 |
A | ALA37 |
A | ASP38 |
A | HOH587 |
A | HOH689 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue EDO A 309 |
Chain | Residue |
A | ASP38 |
A | LYS58 |
A | GLU62 |
A | LEU65 |
A | GLN68 |
A | HIS116 |
A | ARG159 |
A | HOH429 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for residue EDO A 310 |
Chain | Residue |
A | ARG19 |
A | ARG40 |
A | PRO149 |
A | GLY150 |
A | ASP151 |
A | HOH588 |
A | HOH600 |
A | HOH691 |
site_id | AD2 |
Number of Residues | 9 |
Details | binding site for residue EDO A 311 |
Chain | Residue |
A | ALA28 |
A | ASN111 |
A | GLN129 |
A | THR140 |
A | GLU141 |
A | HOH414 |
A | HOH416 |
A | HOH491 |
A | HOH534 |
site_id | AD3 |
Number of Residues | 14 |
Details | binding site for residue 4D6 A 312 |
Chain | Residue |
A | ARG14 |
A | CYS44 |
A | SER45 |
A | ASN79 |
A | SER105 |
A | ASN107 |
A | PRO142 |
A | ASN145 |
A | LYS209 |
A | THR210 |
A | GLY211 |
A | SER212 |
A | GLY214 |
A | HOH403 |
Functional Information from PROSITE/UniProt
site_id | PS00146 |
Number of Residues | 16 |
Details | BETA_LACTAMASE_A Beta-lactamase class-A active site. FaMCSTsKvmaAAAVL |
Chain | Residue | Details |
A | PHE41-LEU56 | |