Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4JKV

Structure of the human smoothened 7TM receptor in complex with an antitumor agent

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 PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 1KS A 601
ChainResidue
AASN219
AARG400
AGLN477
ATRP480
AGLU481
APRO513
AGLU518
AASN521
ALEU522
ALEU221
ATRP281
AASP384
AVAL386
ASER387
APHE391
ATYR394
ALYS395

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OLC A 602
ChainResidue
AGLU447
AARG451
ATHR534

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OLC A 603
ChainResidue
ATYR397
AARG398
AALA401
AALA406
APHE474
BALA377

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OLC A 604
ChainResidue
ASER468
ATYR472
APHE475
AASN476

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE OLA A 605
ChainResidue
AGLY288
AILE316

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OLA A 606
ChainResidue
ATYR323
AHIS361
ATRP365

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG A 607
ChainResidue
APRO220
ALEU221

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGE A 608
ChainResidue
AGLN380
AASN396
ATYR399
AHOH714
BASN396
BTYR399

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PG4 A 609
ChainResidue
AASP229
ATYR233
ALYS519

site_idBC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 1KS B 601
ChainResidue
BASN219
BLEU221
BMET230
BTRP281
BMET301
BASP384
BVAL386
BSER387
BPHE391
BTYR394
BLYS395
BARG400
BGLN477
BTRP480
BGLU481
BPRO513
BGLU518
BASN521
BLEU522

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OLC B 602
ChainResidue
BASP287
BGLU292
BILE293

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE OLC B 603
ChainResidue
BTYR233
BLYS519

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE OLA B 604
ChainResidue
BILE413
BTYR417

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG B 605
ChainResidue
BTHR311
BLEU312
BSER313
BHOH759

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: axial binding residue
ChainResidueDetails
ATRP7
AILE102
BTRP7
BILE102

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
AILE234-ALA254
BILE234-ALA254

site_idSWS_FT_FI3
Number of Residues112
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AASP255-TYR262
ATHR336-SER358
AMET424-ARG451
BASP255-TYR262
BTHR336-SER358
BMET424-ARG451

site_idSWS_FT_FI4
Number of Residues40
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
APRO263-ALA283
BPRO263-ALA283

site_idSWS_FT_FI5
Number of Residues206
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
AGLN284-CYS314
AGLN380-GLY402
AASP473-ALA524
BGLN284-CYS314
BGLN380-GLY402
BASP473-ALA524

site_idSWS_FT_FI6
Number of Residues40
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
AVAL315-LEU335
BVAL315-LEU335

site_idSWS_FT_FI7
Number of Residues40
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
ATYR359-ALA379
BTYR359-ALA379

site_idSWS_FT_FI8
Number of Residues40
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
APHE403-VAL423
BPHE403-VAL423

site_idSWS_FT_FI9
Number of Residues40
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
ALEU452-TYR472
BLEU452-TYR472

site_idSWS_FT_FI10
Number of Residues40
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
AMET525-TRP545
BMET525-TRP545

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

site_idSWS_FT_FI12
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN309
BASN309

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon