Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
A | 0016052 | biological_process | carbohydrate catabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0050525 | molecular_function | cutinase activity |
A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
Functional Information from PROSITE/UniProt
site_id | PS00155 |
Number of Residues | 13 |
Details | CUTINASE_1 Cutinase, serine active site. PnAaIVsGGYSQG |
Chain | Residue | Details |
A | PRO126-GLY138 | |
site_id | PS00931 |
Number of Residues | 18 |
Details | CUTINASE_2 Cutinase, aspartate and histidine active sites. CdiaDaVCyGTlfIlpaH |
Chain | Residue | Details |
A | CYS187-HIS204 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"18983850","evidenceCode":"ECO:0000305"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"evidences":[{"source":"PubMed","id":"18983850","evidenceCode":"ECO:0000305"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"18983850","evidenceCode":"ECO:0000305"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00590","evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1agy |
Chain | Residue | Details |
A | SER136 | |
A | HIS204 | |
A | GLN137 | |
A | SER57 | |
A | ASP191 | |