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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6VRH

Cryo-EM structure of the wild-type human serotonin transporter complexed with 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
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
A0035725biological_processsodium ion transmembrane transport
A0042310biological_processvasoconstriction
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
A0060179biological_processmale mating behavior
A0070161cellular_componentanchoring junction
A0070527biological_processplatelet aggregation
A0071300biological_processcellular response to retinoic acid
A0071321biological_processcellular response to cGMP
A0090067biological_processregulation of thalamus size
A0098810biological_processneurotransmitter reuptake
A0099154cellular_componentserotonergic synapse
A1990708biological_processconditioned place preference
C0002250biological_processadaptive immune response
C0002376biological_processimmune system process
C0019814cellular_componentimmunoglobulin complex
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 Residues24
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"27049939","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues158
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"27049939","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues81
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"27049939","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"27049939","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"27049939","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"27049939","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"27049939","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"27049939","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PubMed","id":"27049939","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PubMed","id":"27049939","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=11","evidences":[{"source":"PubMed","id":"27049939","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=12","evidences":[{"source":"PubMed","id":"27049939","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q7K4Y6","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"34851672","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7LIA","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34851672","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27049939","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7LIA","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"5I6X","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34851672","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7MGW","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27049939","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5I6X","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q7K4Y6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34851672","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7LIA","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"7MGW","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34851672","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7LIA","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"21992875","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PKG","evidences":[{"source":"PubMed","id":"17913921","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27049939","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

240971

PDB entries from 2025-08-27

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