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6BQH

Crystal structure of 5-HT2C in complex with ritanserin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004993molecular_functionG protein-coupled serotonin receptor activity
A0005506molecular_functioniron ion binding
A0005886cellular_componentplasma membrane
A0007186biological_processG protein-coupled receptor signaling pathway
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue E2J A 1201
ChainResidue
ATRP130
APHE223
APHE320
APHE327
APHE328
AASN351
AVAL354
ATYR358
AHOH1301
AASP134
AVAL135
ASER138
ATHR139
AILE142
AVAL215
AGLY218
ASER219

site_idAC2
Number of Residues4
Detailsbinding site for residue OLC A 1202
ChainResidue
ATRP55
ALEU349
APHE353
AOLC1203

site_idAC3
Number of Residues3
Detailsbinding site for residue OLC A 1203
ChainResidue
ALEU333
AMET346
AOLC1202

site_idAC4
Number of Residues4
Detailsbinding site for residue OLC A 1204
ChainResidue
AMET76
ATYR382
AASN386
ATYR387

site_idAC5
Number of Residues3
Detailsbinding site for residue OLC A 1206
ChainResidue
ATHR228
AILE229
AILE232

site_idAC6
Number of Residues2
Detailsbinding site for residue OLC A 1207
ChainResidue
ACYS146
AVAL221

site_idAC7
Number of Residues5
Detailsbinding site for residue PEG A 1208
ChainResidue
ALEU370
APHE371
AARG376
AARG376
AARG377

site_idAC8
Number of Residues5
Detailsbinding site for residue OLA A 1210
ChainResidue
ATYR90
AMET93
AILE97
AILE172
ATRP179

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASImHLCAISLDRYVaI
ChainResidueDetails
AALA140-ILE156

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues25
DetailsTRANSMEM: Helical; Name=1 => ECO:0000250
ChainResidueDetails
AGLN53-VAL78

site_idSWS_FT_FI2
Number of Residues29
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250
ChainResidueDetails
ASER79-ASN89
AASP151-LYS170

site_idSWS_FT_FI3
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000250
ChainResidueDetails
ATYR90-SER110

site_idSWS_FT_FI4
Number of Residues49
DetailsTOPO_DOM: Extracellular => ECO:0000250
ChainResidueDetails
ALEU111-CYS127
ALEU194-ASN213
ASER334-LYS348

site_idSWS_FT_FI5
Number of Residues22
DetailsTRANSMEM: Helical; Name=3 => ECO:0000250
ChainResidueDetails
APRO128-LEU150

site_idSWS_FT_FI6
Number of Residues22
DetailsTRANSMEM: Helical; Name=4 => ECO:0000250
ChainResidueDetails
AALA171-GLY193

site_idSWS_FT_FI7
Number of Residues21
DetailsTRANSMEM: Helical; Name=5 => ECO:0000250
ChainResidueDetails
APHE214-CYS235

site_idSWS_FT_FI8
Number of Residues21
DetailsTRANSMEM: Helical; Name=6 => ECO:0000250
ChainResidueDetails
AVAL312-LEU333

site_idSWS_FT_FI9
Number of Residues22
DetailsTRANSMEM: Helical; Name=7 => ECO:0000250
ChainResidueDetails
ALEU349-PHE371

site_idSWS_FT_FI10
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P41595
ChainResidueDetails
AASP134
ATHR139
ALEU209

site_idSWS_FT_FI11
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN204

site_idSWS_FT_FI12
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
ATRP1007
AILE1102

218853

PDB entries from 2024-04-24

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