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 |
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 | 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 | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 4 |
Chain | Residue |
B | ARG172 |
B | ILE180 |
B | THR181 |
B | HOH331 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 5 |
Chain | Residue |
A | GOL3 |
A | ARG172 |
A | VAL179 |
A | ILE180 |
A | THR181 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SO4 A 6 |
Chain | Residue |
A | SO411 |
A | ARG252 |
A | LYS297 |
B | ARG209 |
B | ALA275 |
B | ARG276 |
B | ALA289 |
B | GLY290 |
B | ALA291 |
B | HOH395 |
B | HOH450 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 7 |
Chain | Residue |
A | ALA275 |
A | ARG288 |
A | ALA289 |
A | GLY290 |
A | ALA291 |
A | HOH411 |
B | ARG252 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 8 |
Chain | Residue |
A | ARG102 |
A | ASN210 |
A | HOH347 |
A | HOH528 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 9 |
Chain | Residue |
A | ARG252 |
B | ARG209 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 10 |
Chain | Residue |
B | ARG102 |
B | GLY211 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 11 |
Chain | Residue |
A | SO46 |
A | ARG252 |
B | ALA275 |
B | ARG276 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 1 |
Chain | Residue |
A | HOH459 |
B | ASP152 |
B | ALA170 |
B | HOH383 |
B | HOH505 |
B | HOH521 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 2 |
Chain | Residue |
A | ASP152 |
A | ASP171 |
A | HOH394 |
B | HOH483 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 3 |
Chain | Residue |
A | SO45 |
A | ARG110 |
A | ARG172 |
A | THR181 |
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
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17999929","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9811546","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P25910","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"9811546","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qh5 |
Chain | Residue | Details |
A | ASP120 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qh5 |
Chain | Residue | Details |
B | ASP120 | |
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 |