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6VRL

Cryo-EM structure of the wild-type human serotonin transporter complexed with I-paroxetine and 8B6 Fab

Functional Information from GO Data
ChainGOidnamespacecontents
A0001666biological_processresponse to hypoxia
A0005178molecular_functionintegrin binding
A0005261molecular_functionmonoatomic cation channel activity
A0005326molecular_functionneurotransmitter transmembrane transporter activity
A0005335molecular_functionserotonin:sodium:chloride symporter activity
A0005515molecular_functionprotein binding
A0005768cellular_componentendosome
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0006836biological_processneurotransmitter transport
A0006837biological_processserotonin transport
A0006865biological_processamino acid transport
A0007584biological_processresponse to nutrient
A0007613biological_processmemory
A0007623biological_processcircadian rhythm
A0008504molecular_functionmonoamine transmembrane transporter activity
A0009410biological_processresponse to xenobiotic stimulus
A0009636biological_processresponse to toxic substance
A0010008cellular_componentendosome membrane
A0010033biological_processobsolete response to organic substance
A0010628biological_processpositive regulation of gene expression
A0012505cellular_componentendomembrane system
A0014064biological_processpositive regulation of serotonin secretion
A0015297molecular_functionantiporter activity
A0015844biological_processmonoamine transport
A0016020cellular_componentmembrane
A0017075molecular_functionsyntaxin-1 binding
A0019811molecular_functioncocaine binding
A0021941biological_processnegative regulation of cerebellar granule cell precursor proliferation
A0031402molecular_functionsodium ion binding
A0032227biological_processnegative regulation of synaptic transmission, dopaminergic
A0032355biological_processresponse to estradiol
A0035176biological_processsocial behavior
A0035725biological_processsodium ion transmembrane transport
A0042310biological_processvasoconstriction
A0042713biological_processsperm ejaculation
A0042734cellular_componentpresynaptic membrane
A0042802molecular_functionidentical protein binding
A0042995cellular_componentcell projection
A0043005cellular_componentneuron projection
A0045121cellular_componentmembrane raft
A0045202cellular_componentsynapse
A0045211cellular_componentpostsynaptic membrane
A0045665biological_processnegative regulation of neuron differentiation
A0045787biological_processpositive regulation of cell cycle
A0046621biological_processnegative regulation of organ growth
A0046872molecular_functionmetal ion binding
A0048148biological_processbehavioral response to cocaine
A0048484biological_processenteric nervous system development
A0048854biological_processbrain morphogenesis
A0050998molecular_functionnitric-oxide synthase binding
A0051015molecular_functionactin filament binding
A0051378molecular_functionserotonin binding
A0051610biological_processserotonin uptake
A0051899biological_processmembrane depolarization
A0070161cellular_componentanchoring junction
A0070527biological_processplatelet aggregation
A0071300biological_processcellular response to retinoic acid
A0071310biological_processobsolete cellular response to organic substance
A0071321biological_processcellular response to cGMP
A0090067biological_processregulation of thalamus size
A0098810biological_processneurotransmitter reuptake
A0099154cellular_componentserotonergic synapse
A1990708biological_processconditioned place preference
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
CTYR212-HIS218

site_idPS00610
Number of Residues15
DetailsNA_NEUROTRAN_SYMP_1 Sodium:neurotransmitter symporter family signature 1. WRFPYicyqNGGGaF
ChainResidueDetails
ATRP103-PHE117

site_idPS00754
Number of Residues21
DetailsNA_NEUROTRAN_SYMP_2 Sodium:neurotransmitter symporter family signature 2. YLisSFTdqLPWtsCknswNT
ChainResidueDetails
ATYR186-THR206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues201
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AMET1-ASP87
AGLU136-GLY160
ALYS272-SER277
AALA348-ASP360
AGLU444-GLU463
AGLY517-ARG538
AARG596-VAL630

site_idSWS_FT_FI2
Number of Residues24
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:27049939
ChainResidueDetails
APHE88-ASN112

site_idSWS_FT_FI3
Number of Residues158
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
AGLY113-GLY115
ALEU187-SER252
AARG298-GLY324
ATHR381-THR421
AGLY484-GLU494
ASER559-SER574

site_idSWS_FT_FI4
Number of Residues19
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:27049939
ChainResidueDetails
AALA116-MET135

site_idSWS_FT_FI5
Number of Residues25
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:27049939
ChainResidueDetails
AILE161-TYR186

site_idSWS_FT_FI6
Number of Residues18
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:27049939
ChainResidueDetails
ATRP253-TRP271

site_idSWS_FT_FI7
Number of Residues19
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:27049939
ChainResidueDetails
AGLY278-VAL297

site_idSWS_FT_FI8
Number of Residues22
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:27049939
ChainResidueDetails
AVAL325-PHE347

site_idSWS_FT_FI9
Number of Residues19
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:27049939
ChainResidueDetails
AALA361-PHE380

site_idSWS_FT_FI10
Number of Residues21
DetailsTRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:27049939
ChainResidueDetails
APHE422-LEU443

site_idSWS_FT_FI11
Number of Residues19
DetailsTRANSMEM: Helical; Name=9 => ECO:0000269|PubMed:27049939
ChainResidueDetails
AARG464-PHE483

site_idSWS_FT_FI12
Number of Residues21
DetailsTRANSMEM: Helical; Name=10 => ECO:0000269|PubMed:27049939
ChainResidueDetails
ATYR495-TYR516

site_idSWS_FT_FI13
Number of Residues19
DetailsTRANSMEM: Helical; Name=11 => ECO:0000269|PubMed:27049939
ChainResidueDetails
AILE539-MET558

site_idSWS_FT_FI14
Number of Residues20
DetailsTRANSMEM: Helical; Name=12 => ECO:0000269|PubMed:27049939
ChainResidueDetails
AILE575-TYR595

site_idSWS_FT_FI15
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q7K4Y6, ECO:0000269|PubMed:34851672, ECO:0000312|PDB:7LIA
ChainResidueDetails
AGLY94
AVAL97
AASP437

site_idSWS_FT_FI16
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:34851672, ECO:0000305|PubMed:27049939, ECO:0000312|PDB:7LIA, ECO:0007744|PDB:5I6X
ChainResidueDetails
AALA96
ASER336

site_idSWS_FT_FI17
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:34851672, ECO:0000312|PDB:7MGW
ChainResidueDetails
AASP98
AGLU494

site_idSWS_FT_FI18
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:27049939, ECO:0007744|PDB:5I6X
ChainResidueDetails
AASN101
AASN368

site_idSWS_FT_FI19
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q7K4Y6
ChainResidueDetails
ALEU434
ASER438

site_idSWS_FT_FI20
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:34851672, ECO:0000312|PDB:7LIA, ECO:0000312|PDB:7MGW
ChainResidueDetails
ATHR439
APHE556
ASER559

site_idSWS_FT_FI21
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:34851672, ECO:0000312|PDB:7LIA
ChainResidueDetails
ATYR495

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:21992875
ChainResidueDetails
ATYR47
ATYR142

site_idSWS_FT_FI23
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKG => ECO:0000269|PubMed:17913921
ChainResidueDetails
ATHR276

site_idSWS_FT_FI24
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:27049939
ChainResidueDetails
AASN208
AASN217

222624

PDB entries from 2024-07-17

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