9W0HFunctional Information from PROSITE/UniProt
| site_id | PS00152 |
| Number of Residues | 10 |
| Details | ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PALDPSRSKS |
| Chain | Residue | Details |
| A | PRO509-SER518 |
| site_id | PS00237 |
| Number of Residues | 17 |
| Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASTcSLLAIAIERYLtM |
| Chain | Residue | Details |
| A | ALA124-MET140 |
| site_id | PS00776 |
| Number of Residues | 11 |
| Details | GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYVVDsW |
| Chain | Residue | Details |
| A | PRO299-TRP309 |
| site_id | PS00777 |
| Number of Residues | 12 |
| Details | GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. MatEGYQSSGsS |
| Chain | Residue | Details |
| A | MET393-SER404 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 184 |
| Details | Domain: {"description":"GH11","evidences":[{"source":"PROSITE-ProRule","id":"PRU01097","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 43 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 18 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 432 |
| Chain | Residue | Details |
| A | ASN259 | modifies pKa |
| A | TYR293 | electrostatic destabiliser |
| A | GLU302 | covalent catalysis, proton shuttle (general acid/base) |
| A | TYR304 | modifies pKa |
| A | GLU396 | proton shuttle (general acid/base) |
