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 | 2 |
Details | BINDING SITE FOR RESIDUE ACT A 2001 |
Chain | Residue |
A | VAL73 |
A | THR176 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT A 2002 |
Chain | Residue |
A | TYR167 |
A | VAL170 |
A | GLY173 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT A 2003 |
Chain | Residue |
A | THR190 |
A | TYR256 |
A | TRP334 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT A 2004 |
Chain | Residue |
A | HIS153 |
A | ASP166 |
A | TYR272 |
A | HIS273 |
A | ASP276 |
A | SER150 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 2005 |
Chain | Residue |
A | PHE36 |
A | TYR164 |
A | LEU226 |
A | TYR272 |
A | HIS333 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ACT A 2006 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT A 2007 |
Chain | Residue |
A | MET228 |
A | GLY231 |
A | ALA232 |
A | HOH2115 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT A 2008 |
Chain | Residue |
A | HIS45 |
A | PRO48 |
A | ALA49 |
A | HIS117 |
A | ASP119 |
A | ASN344 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT A 2009 |
Chain | Residue |
A | GLY94 |
A | GLU96 |
A | HOH2132 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 101 |
Details | Domain: {"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"18585390","evidenceCode":"ECO:0000305"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"18585390","evidenceCode":"ECO:0000305"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Site: {"description":"Contributes to the formation of an oxyanion binding site for the epoxide oxygen of substrate","evidences":[{"source":"PubMed","id":"18585390","evidenceCode":"ECO:0000305"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Site: {"description":"Plays an orienting role for the imidazole group of His-333","evidences":[{"source":"PubMed","id":"18585390","evidenceCode":"ECO:0000305"}]} |
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 | |