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 |
A | 0046872 | molecular_function | metal ion binding |
B | 0008800 | molecular_function | beta-lactamase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0017001 | biological_process | antibiotic catabolic process |
B | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
B | 0046677 | biological_process | response to antibiotic |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | binding site for residue NXL A 301 |
Chain | Residue |
A | CYS69 |
A | THR235 |
A | GLY236 |
A | SER237 |
A | ARG276 |
A | HOH401 |
A | HOH429 |
A | HOH438 |
A | HOH467 |
A | HOH624 |
A | HOH661 |
A | SER70 |
A | ASN104 |
A | TYR105 |
A | SER130 |
A | ASN132 |
A | ASN170 |
A | THR216 |
A | LYS234 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue PO4 A 302 |
Chain | Residue |
A | LYS111 |
A | HOH414 |
A | HOH420 |
A | HOH436 |
A | HOH440 |
A | HOH610 |
B | LYS38 |
B | HOH688 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue NA A 303 |
Chain | Residue |
A | GLY238 |
A | HOH445 |
A | HOH509 |
A | HOH605 |
A | HOH646 |
A | HOH712 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue K A 304 |
Chain | Residue |
A | PRO107 |
A | GLU110 |
A | LYS111 |
A | HOH769 |
B | HOH556 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue K A 305 |
Chain | Residue |
A | ARG222 |
A | TRP229 |
A | HOH416 |
A | HOH578 |
A | HOH579 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue K A 306 |
Chain | Residue |
A | GLN128 |
A | HOH427 |
A | HOH512 |
B | HOH818 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue K A 307 |
Chain | Residue |
A | GLY147 |
A | ALA150 |
A | HOH719 |
A | HOH755 |
A | HOH825 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue K A 308 |
Chain | Residue |
A | GLY156 |
A | HOH644 |
A | HOH792 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue K A 309 |
Chain | Residue |
A | PRO268 |
A | HOH434 |
A | HOH609 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue K A 310 |
Chain | Residue |
A | THR215 |
A | THR216 |
A | HOH411 |
B | HOH659 |
B | HOH755 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue NA A 311 |
Chain | Residue |
A | TYR105 |
A | HOH467 |
A | HOH688 |
B | THR227 |
B | TRP229 |
B | HOH533 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue NA A 312 |
Chain | Residue |
A | TYR129 |
A | HOH688 |
A | HOH831 |
B | HOH519 |
B | HOH755 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue PO4 B 302 |
Chain | Residue |
B | LYS88 |
B | THR202 |
B | GLN203 |
B | HOH417 |
B | HOH431 |
B | HOH785 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue NA B 303 |
Chain | Residue |
B | GLY238 |
B | HOH449 |
B | HOH563 |
B | HOH626 |
B | HOH634 |
B | HOH714 |
site_id | AD6 |
Number of Residues | 1 |
Details | binding site for residue K B 304 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue K B 305 |
Chain | Residue |
B | ASP53 |
B | HOH607 |
B | HOH740 |
B | HOH823 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue K B 306 |
Chain | Residue |
B | ARG222 |
B | LEU225 |
B | THR227 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue K B 307 |
Chain | Residue |
B | HOH593 |
A | HOH448 |
B | SER228 |
B | THR230 |
B | GLN254 |
B | HOH518 |
site_id | AE1 |
Number of Residues | 5 |
Details | binding site for residue K B 308 |
Chain | Residue |
B | ARG276 |
B | ASP277 |
B | HOH605 |
B | HOH717 |
B | HOH721 |
site_id | AE2 |
Number of Residues | 4 |
Details | binding site for residue K B 309 |
Chain | Residue |
B | PRO167 |
B | HOH641 |
B | HOH725 |
B | HOH849 |
site_id | AE3 |
Number of Residues | 22 |
Details | binding site for Di-peptide NXL B 301 and SER B 70 |
Chain | Residue |
A | ARG222 |
B | MET68 |
B | CYS69 |
B | THR71 |
B | SER72 |
B | LYS73 |
B | ASN104 |
B | TYR105 |
B | SER130 |
B | ASN132 |
B | ASN170 |
B | THR216 |
B | LYS234 |
B | THR235 |
B | GLY236 |
B | SER237 |
B | ARG276 |
B | HOH403 |
B | HOH429 |
B | HOH447 |
B | HOH575 |
B | HOH641 |
site_id | AE4 |
Number of Residues | 22 |
Details | binding site for Di-peptide NXL B 301 and SER B 70 |
Chain | Residue |
A | ARG222 |
B | MET68 |
B | CYS69 |
B | THR71 |
B | SER72 |
B | LYS73 |
B | ASN104 |
B | TYR105 |
B | SER130 |
B | ASN132 |
B | ASN170 |
B | THR216 |
B | LYS234 |
B | THR235 |
B | GLY236 |
B | SER237 |
B | ARG276 |
B | HOH403 |
B | HOH429 |
B | HOH447 |
B | HOH575 |
B | HOH641 |
site_id | AE5 |
Number of Residues | 22 |
Details | binding site for Di-peptide NXL B 301 and SER B 70 |
Chain | Residue |
A | ARG222 |
B | MET68 |
B | CYS69 |
B | THR71 |
B | SER72 |
B | LYS73 |
B | ASN104 |
B | TYR105 |
B | SER130 |
B | ASN132 |
B | ASN170 |
B | THR216 |
B | LYS234 |
B | THR235 |
B | GLY236 |
B | SER237 |
B | ARG276 |
B | HOH403 |
B | HOH429 |
B | HOH447 |
B | HOH575 |
B | HOH641 |
Functional Information from PROSITE/UniProt
site_id | PS00146 |
Number of Residues | 16 |
Details | BETA_LACTAMASE_A Beta-lactamase class-A active site. FpMCSTsKvmaAAAVL |
Chain | Residue | Details |
A | PHE66-LEU81 | |