Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0004994 | molecular_function | somatostatin receptor activity |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0031176 | molecular_function | endo-1,4-beta-xylanase activity |
| A | 0045493 | biological_process | xylan catabolic process |
Functional Information from PROSITE/UniProt
| site_id | PS00237 |
| Number of Residues | 17 |
| Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. TSIfCLTVMSIDRYLaV |
| Chain | Residue | Details |
| A | THR128-VAL144 | |
| site_id | PS00776 |
| Number of Residues | 11 |
| Details | GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYVVDsW |
| Chain | Residue | Details |
| A | PRO1074-TRP1084 | |
| site_id | PS00777 |
| Number of Residues | 12 |
| Details | GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. MatEGYQSSGsS |
| Chain | Residue | Details |
| A | MET1168-SER1179 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 27 |
| Details | Signal: {} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 184 |
| Details | Domain: {"description":"GH11","evidences":[{"source":"PROSITE-ProRule","id":"PRU01097","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10062","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8019418","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10063","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8019418","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 32 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 48 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 19 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 19 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 14 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for ligand binding"} |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 432 |
| Chain | Residue | Details |
| A | ASN1034 | modifies pKa |
| A | TYR1068 | electrostatic destabiliser |
| A | GLU1077 | covalent catalysis, proton shuttle (general acid/base) |
| A | TYR1079 | modifies pKa |
| A | GLU1171 | proton shuttle (general acid/base) |
