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5L7I

Structure of human Smoothened in complex with Vismodegib

Functional Information from GO Data
ChainGOidnamespacecontents
A0004888molecular_functiontransmembrane signaling receptor activity
A0005506molecular_functioniron ion binding
A0007166biological_processcell surface receptor signaling pathway
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0004888molecular_functiontransmembrane signaling receptor activity
B0005506molecular_functioniron ion binding
B0007166biological_processcell surface receptor signaling pathway
B0009055molecular_functionelectron transfer activity
B0016020cellular_componentmembrane
B0020037molecular_functionheme binding
B0022900biological_processelectron transport chain
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
AILE234-ALA254
BILE234-ALA254

site_idSWS_FT_FI2
Number of Residues58
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AASP255-TYR262
ATHR336-SER358
BASP255-TYR262
BTHR336-SER358

site_idSWS_FT_FI3
Number of Residues40
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
APRO263-ALA283
BPRO263-ALA283

site_idSWS_FT_FI4
Number of Residues206
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
AGLN284-CYS314
AGLN380-GLY402
AASP473-ALA524
BGLN284-CYS314
BGLN380-GLY402
BASP473-ALA524

site_idSWS_FT_FI5
Number of Residues40
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
AVAL315-LEU335
BVAL315-LEU335

site_idSWS_FT_FI6
Number of Residues40
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
ATYR359-ALA379
BTYR359-ALA379

site_idSWS_FT_FI7
Number of Residues40
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
APHE403-VAL423
BPHE403-VAL423

site_idSWS_FT_FI8
Number of Residues40
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
ALEU452-TYR472
BLEU452-TYR472

site_idSWS_FT_FI9
Number of Residues40
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
AMET525-TRP545
BMET525-TRP545

site_idSWS_FT_FI10
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:35658032, ECO:0007744|PDB:7ZI0
ChainResidueDetails
AASP95
BASP95

site_idSWS_FT_FI11
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P56726
ChainResidueDetails
ATYR394
BTYR394

site_idSWS_FT_FI12
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN35
AASN188
AASN309
BASN35
BASN188
BASN309

site_idSWS_FT_FI13
Number of Residues4
DetailsBINDING: axial binding residue
ChainResidueDetails
ATRP1022
AILE1117
BTRP1022
BILE1117

225399

PDB entries from 2024-09-25

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