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5V57

3.0A SYN structure of the multi-domain human smoothened receptor in complex with TC114

Functional Information from GO Data
ChainGOidnamespacecontents
A0004888molecular_functiontransmembrane signaling receptor activity
A0007166biological_processcell surface receptor signaling pathway
A0009055molecular_functionelectron transfer activity
A0010181molecular_functionFMN binding
A0016020cellular_componentmembrane
B0004888molecular_functiontransmembrane signaling receptor activity
B0007166biological_processcell surface receptor signaling pathway
B0009055molecular_functionelectron transfer activity
B0010181molecular_functionFMN binding
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue 836 A 1201
ChainResidue
AASN219
ALYS395
AARG400
AGLN477
ATRP480
AGLU481
APHE484
APRO513
AGLU518
AASN521
ALEU522
ALEU221
AMET230
ATRP281
AASP384
AVAL386
ASER387
APHE391
ATYR394

site_idAC2
Number of Residues18
Detailsbinding site for residue FMN A 1202
ChainResidue
ASER1010
ATHR1011
ATHR1012
AGLY1013
AASN1014
ATHR1015
ASER1058
ATHR1059
ATRP1060
AGLY1061
ACYS1093
AGLY1094
AASP1095
ATRP1098
AGLU1099
ATYR1100
APHE1101
ACYS1102

site_idAC3
Number of Residues17
Detailsbinding site for residue 836 B 1201
ChainResidue
BASN219
BLEU221
BMET230
BASP384
BVAL386
BPHE391
BTYR394
BLYS395
BARG400
BGLN477
BTRP480
BGLU481
BPHE484
BPRO513
BGLU518
BASN521
BLEU522

site_idAC4
Number of Residues17
Detailsbinding site for residue FMN B 1202
ChainResidue
BSER1010
BTHR1011
BTHR1012
BGLY1013
BASN1014
BTHR1015
BSER1058
BTHR1059
BTRP1060
BGLY1061
BCYS1093
BGLY1094
BASP1095
BTRP1098
BTYR1100
BPHE1101
BCYS1102

site_idAC5
Number of Residues7
Detailsbinding site for residue OLC B 1203
ChainResidue
BTRP339
BPHE343
BLEU346
BILE445
BASN446
BMET449
BLEU450

Functional Information from PROSITE/UniProt
site_idPS00201
Number of Residues17
DetailsFLAVODOXIN Flavodoxin signature. IVYgSTtGnTEytAEtI
ChainResidueDetails
AILE1006-ILE1022

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 Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P56726
ChainResidueDetails
ASER556
BSER556

site_idSWS_FT_FI13
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN188
AASN309
BASN188
BASN309

229183

PDB entries from 2024-12-18

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