Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008270 | molecular_function | zinc ion binding |
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 | 0042597 | cellular_component | periplasmic space |
A | 0046677 | biological_process | response to antibiotic |
A | 0046872 | molecular_function | metal ion binding |
B | 0008270 | molecular_function | zinc 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 | 0042597 | cellular_component | periplasmic space |
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 | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 320 |
Chain | Residue |
A | HIS116 |
A | HIS118 |
A | HIS196 |
A | SO41106 |
A | HOH1308 |
A | HOH1311 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 321 |
Chain | Residue |
B | SO41105 |
B | HOH1296 |
B | HOH1313 |
B | HIS116 |
B | HIS118 |
B | HIS196 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 1101 |
Chain | Residue |
B | ARG172 |
B | VAL179 |
B | ILE180 |
B | THR181 |
B | HOH1171 |
B | HOH1307 |
B | HOH1319 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1102 |
Chain | Residue |
A | ARG172 |
A | VAL179 |
A | ILE180 |
A | THR181 |
A | HOH1316 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 1103 |
Chain | Residue |
A | ARG102 |
A | HOH1158 |
A | HOH1212 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 1104 |
Chain | Residue |
A | ARG209 |
A | ALA275 |
A | ARG276 |
A | ALA289 |
A | GLY290 |
A | ALA291 |
A | HOH1274 |
A | HOH1288 |
A | HOH1298 |
B | HOH1419 |
site_id | AC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SO4 B 1105 |
Chain | Residue |
B | HIS196 |
B | SER221 |
B | SER225 |
B | PRO227 |
B | HIS263 |
B | ZN321 |
B | HOH1296 |
B | HOH1298 |
B | HOH1313 |
B | HOH1347 |
B | HOH1355 |
site_id | AC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE SO4 A 1106 |
Chain | Residue |
A | HIS196 |
A | SER221 |
A | SER225 |
A | PRO227 |
A | HIS263 |
A | ZN320 |
A | HOH1194 |
A | HOH1308 |
A | HOH1310 |
A | HOH1311 |
A | HOH1389 |
A | HOH1424 |
Functional Information from PROSITE/UniProt
site_id | PS00743 |
Number of Residues | 21 |
Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. LlSHaHADhaGPvaelkrrtG |
Chain | Residue | Details |
A | LEU113-GLY133 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS116 | |
A | HIS196 | |
B | HIS116 | |
B | HIS118 | |
B | ASP120 | |
B | HIS121 | |
B | HIS196 | |
A | HIS118 | |
A | ASP120 | |
A | HIS121 | |
Chain | Residue | Details |
A | ASP220 | |
B | ASP220 | |
Chain | Residue | Details |
A | HIS263 | |
B | HIS263 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 258 |
Chain | Residue | Details |
A | HIS116 | metal ligand |
A | HIS118 | metal ligand |
A | ASP120 | metal ligand |
A | HIS121 | metal ligand |
A | HIS196 | metal ligand |
A | TYR229 | electrostatic stabiliser, hydrogen bond donor |
A | HIS263 | metal ligand |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 258 |
Chain | Residue | Details |
B | HIS116 | metal ligand |
B | HIS118 | metal ligand |
B | ASP120 | metal ligand |
B | HIS121 | metal ligand |
B | HIS196 | metal ligand |
B | TYR229 | electrostatic stabiliser, hydrogen bond donor |
B | HIS263 | metal ligand |