6D32
Crystal structure of Xenopus Smoothened in complex with cyclopamine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004888 | molecular_function | transmembrane signaling receptor activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0007166 | biological_process | cell surface receptor signaling pathway |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016020 | cellular_component | membrane |
| A | 0020037 | molecular_function | heme binding |
| A | 0022900 | biological_process | electron transport chain |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CY8 A 1201 |
| Chain | Residue |
| A | ASP68 |
| A | LEU81 |
| A | TRP82 |
| A | GLU133 |
| A | ARG134 |
| A | GLU471 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue CY8 A 1202 |
| Chain | Residue |
| A | LYS368 |
| A | GLN450 |
| A | GLU454 |
| A | GLU491 |
| A | ASN192 |
| A | ASP357 |
| A | TYR367 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"29804838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6D32","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6D35","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29804838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6D32","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6D35","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"29804838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6D32","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6D35","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 82 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"29804838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6D32","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6D35","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"29804838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6D32","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6D35","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 19 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"29804838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6D32","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6D35","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"29804838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6D32","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6D35","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"29804838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6D32","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6D35","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"29804838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6D32","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6D35","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 116 |
| Details | Domain: {"description":"FZ","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27545348","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29804838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6D35","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P56726","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Lipidation: {"description":"Cholesterol aspartate ester","evidences":[{"source":"UniProtKB","id":"Q99835","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
