Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0030599 | molecular_function | pectinesterase activity |
| A | 0042545 | biological_process | cell wall modification |
| B | 0004857 | molecular_function | enzyme inhibitor activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0043086 | biological_process | negative regulation of catalytic activity |
| B | 0046910 | molecular_function | pectinesterase inhibitor activity |
Functional Information from PROSITE/UniProt
| site_id | PS00503 |
| Number of Residues | 10 |
| Details | PECTINESTERASE_2 Pectinesterase signature 2. VtGTVDFIFG |
| Chain | Residue | Details |
| A | VAL148-GLY157 | |
| site_id | PS00800 |
| Number of Residues | 20 |
| Details | PECTINESTERASE_1 Pectinesterase signature 1. SktryviYVKrGTYKEnveV |
| Chain | Residue | Details |
| A | SER29-VAL48 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10040","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10040","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1gq8 |
| Chain | Residue | Details |
| A | GLN109 | |
| A | GLN131 | |
| A | ASP132 | |
| A | ASP153 | |
