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 | 0042597 | cellular_component | periplasmic space |
A | 0046677 | biological_process | response to antibiotic |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 1 |
Chain | Residue |
A | ASP120 |
A | CYS221 |
A | HOH227 |
A | HIS263 |
A | SO4311 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 2 |
Chain | Residue |
A | HOH519 |
A | HIS118 |
A | HIS196 |
A | SO4311 |
A | HOH464 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 3 |
Chain | Residue |
A | HIS289 |
A | GLU292 |
A | CL308 |
A | CL309 |
A | CL310 |
A | HOH518 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 308 |
Chain | Residue |
A | ZN3 |
A | CL309 |
A | HOH518 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 309 |
Chain | Residue |
A | ZN3 |
A | GLU292 |
A | LEU293 |
A | CL308 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 310 |
Chain | Residue |
A | ZN3 |
A | HIS289 |
A | GLY290 |
A | GLU292 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL A 4 |
Chain | Residue |
A | HOH14 |
A | ASN116 |
A | GLY200 |
A | CYS221 |
A | ILE222 |
A | HOH345 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 5 |
Chain | Residue |
A | SER104 |
A | LYS106 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 6 |
Chain | Residue |
A | SER104 |
A | ARG105 |
A | HOH413 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 7 |
Chain | Residue |
A | ARG158 |
A | HOH423 |
site_id | BC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 311 |
Chain | Residue |
A | ZN1 |
A | ZN2 |
A | HIS118 |
A | ASP120 |
A | HIS196 |
A | HOH227 |
A | HIS263 |
A | HOH363 |
A | HOH464 |
A | HOH499 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 312 |
Chain | Residue |
A | HOH32 |
A | HOH62 |
A | LYS97 |
A | ARG102 |
A | LYS257 |
A | HOH438 |
A | HOH500 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 313 |
Chain | Residue |
A | LYS129 |
A | VAL170 |
A | LEU171 |
A | LYS302 |
A | HOH400 |
A | HOH476 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 314 |
Chain | Residue |
A | ARG140 |
A | ARG140 |
A | HOH332 |
A | HOH332 |
A | HOH395 |
A | HOH395 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 315 |
Chain | Residue |
A | HIS176 |
A | ASP177 |
A | GLY178 |
A | ASP179 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 316 |
Chain | Residue |
A | ARG143 |
A | ARG143 |
A | LYS147 |
A | LYS147 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 317 |
Chain | Residue |
A | ARG158 |
A | PRO165 |
A | ASP166 |
A | HOH387 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 318 |
Chain | Residue |
A | LYS78 |
A | LEU182 |
A | GLN183 |
A | GLU184 |
A | HOH329 |
A | HOH343 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 319 |
Chain | Residue |
A | ASP179 |
A | ARG188 |
A | PHE190 |
A | HOH331 |
A | HOH511 |
site_id | CC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 320 |
Chain | Residue |
A | LEU231 |
A | GLY232 |
A | HOH424 |
Functional Information from PROSITE/UniProt
site_id | PS00743 |
Number of Residues | 20 |
Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. InTNyHTDraGGnaywksi.G |
Chain | Residue | Details |
A | ILE113-GLY133 | |
site_id | PS00744 |
Number of Residues | 13 |
Details | BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PdeqVLyGgCILK |
Chain | Residue | Details |
A | PRO209-LYS224 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP120 | |
A | CYS221 | |
A | HIS263 | |
Chain | Residue | Details |
A | THR157 | |
Chain | Residue | Details |
A | HIS196 | |
Chain | Residue | Details |
A | LYS224 | |
Chain | Residue | Details |
A | ASN233 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
A | ASP120 | |
A | ASN233 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
A | ASP120 | |