5L7I
Structure of human Smoothened in complex with Vismodegib
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 |
A | 0042597 | cellular_component | periplasmic space |
A | 0046872 | molecular_function | metal ion binding |
B | 0004888 | molecular_function | transmembrane signaling receptor activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0007166 | biological_process | cell surface receptor signaling pathway |
B | 0009055 | molecular_function | electron transfer activity |
B | 0016020 | cellular_component | membrane |
B | 0020037 | molecular_function | heme binding |
B | 0022900 | biological_process | electron transport chain |
B | 0042597 | cellular_component | periplasmic space |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000255 |
Chain | Residue | Details |
A | ILE234-ALA254 | |
B | ILE234-ALA254 |
site_id | SWS_FT_FI2 |
Number of Residues | 58 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | ASP255-TYR262 | |
A | THR336-SER358 | |
B | ASP255-TYR262 | |
B | THR336-SER358 |
site_id | SWS_FT_FI3 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000255 |
Chain | Residue | Details |
A | PRO263-ALA283 | |
B | PRO263-ALA283 |
site_id | SWS_FT_FI4 |
Number of Residues | 206 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
A | GLN284-CYS314 | |
A | GLN380-GLY402 | |
A | ASP473-ALA524 | |
B | GLN284-CYS314 | |
B | GLN380-GLY402 | |
B | ASP473-ALA524 |
site_id | SWS_FT_FI5 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000255 |
Chain | Residue | Details |
A | VAL315-LEU335 | |
B | VAL315-LEU335 |
site_id | SWS_FT_FI6 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000255 |
Chain | Residue | Details |
A | TYR359-ALA379 | |
B | TYR359-ALA379 |
site_id | SWS_FT_FI7 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000255 |
Chain | Residue | Details |
A | PHE403-VAL423 | |
B | PHE403-VAL423 |
site_id | SWS_FT_FI8 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000255 |
Chain | Residue | Details |
A | LEU452-TYR472 | |
B | LEU452-TYR472 |
site_id | SWS_FT_FI9 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000255 |
Chain | Residue | Details |
A | MET525-TRP545 | |
B | MET525-TRP545 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:35658032, ECO:0007744|PDB:7ZI0 |
Chain | Residue | Details |
A | ASP95 | |
B | ASP95 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P56726 |
Chain | Residue | Details |
A | TYR394 | |
B | TYR394 |
site_id | SWS_FT_FI12 |
Number of Residues | 6 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN35 | |
A | ASN188 | |
A | ASN309 | |
B | ASN35 | |
B | ASN188 | |
B | ASN309 |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | TRP1022 | |
A | ILE1117 | |
B | TRP1022 | |
B | ILE1117 |