Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004301 | molecular_function | epoxide hydrolase activity |
A | 0009636 | biological_process | response to toxic substance |
A | 0016787 | molecular_function | hydrolase activity |
A | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 357 |
Chain | Residue |
A | PRO37 |
A | THR190 |
A | TYR256 |
A | TRP334 |
A | GLN337 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT A 358 |
Chain | Residue |
A | ARG63 |
A | GLU81 |
A | THR176 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT A 359 |
Chain | Residue |
A | ASP166 |
A | ALA169 |
A | TYR272 |
A | ASP276 |
A | HOH367 |
A | HIS153 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BSU A 360 |
Chain | Residue |
A | PHE36 |
A | ASP104 |
A | TRP105 |
A | ILE137 |
A | TYR164 |
A | LEU189 |
A | TYR272 |
A | HIS333 |
A | TRP334 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP104 | |
Chain | Residue | Details |
A | HIS333 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Contributes to the formation of an oxyanion binding site for the epoxide oxygen of substrate => ECO:0000305|PubMed:18585390 |
Chain | Residue | Details |
A | TYR164 | |
A | TYR272 | |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Plays an orienting role for the imidazole group of His-333 => ECO:0000305|PubMed:18585390 |
Chain | Residue | Details |
A | ASP302 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b6g |
Chain | Residue | Details |
A | ASP302 | |
A | ASP104 | |
A | HIS333 | |