Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0102007 | molecular_function | acyl-L-homoserine-lactone lactonohydrolase activity |
A | 1901335 | biological_process | lactone catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 301 |
Chain | Residue |
A | ASP108 |
A | HIS109 |
A | ASP191 |
A | HIS235 |
A | ZN302 |
A | HOH401 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 302 |
Chain | Residue |
A | ASP191 |
A | ZN301 |
A | HOH401 |
A | HIS104 |
A | HIS106 |
A | HIS169 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 303 |
Chain | Residue |
A | LYS29 |
A | LEU30 |
A | ARG89 |
A | PHE246 |
A | HOH471 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 304 |
Chain | Residue |
A | GLU61 |
A | LYS76 |
A | MET77 |
A | THR78 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 305 |
Chain | Residue |
A | HIS145 |
A | ASN147 |
A | LYS226 |
A | HOH407 |
A | HOH517 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 306 |
Chain | Residue |
A | ALA115 |
A | GLU152 |
A | GLY153 |
A | TYR165 |
A | HOH411 |
A | HOH424 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 307 |
Chain | Residue |
A | GLU61 |
A | GLY62 |
A | ASN65 |
A | LEU74 |
A | TYR249 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 7 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |