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4XPT

X-ray structure of Drosophila dopamine transporter with subsiteB mutations D121G/S426M and EL2 deletion of 162-201 in complex with substrate analogue 3,4 dichlorophen ethylamine

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
LTYR193-HIS199

site_idPS00610
Number of Residues15
DetailsNA_NEUROTRAN_SYMP_1 Sodium:neurotransmitter symporter family signature 1. WRFPYlcykNGGGaF
ChainResidueDetails
ATRP51-PHE65

site_idPS00754
Number of Residues21
DetailsNA_NEUROTRAN_SYMP_2 Sodium:neurotransmitter symporter family signature 2. FFfaSFTnsLPWtsCnniwNT
ChainResidueDetails
APHE134-THR154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues25
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25961798, ECO:0000269|PubMed:25970245
ChainResidueDetails
AVAL34-LYS59

site_idSWS_FT_FI2
Number of Residues164
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25961798, ECO:0000269|PubMed:25970245
ChainResidueDetails
AASN60-GLY63
APHE139-VAL275
APHE325-THR348
APHE405-ARG444
AILE507
AGLN588-PHE590

site_idSWS_FT_FI3
Number of Residues23
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25961798, ECO:0000269|PubMed:25970245
ChainResidueDetails
AALA64-LEU87

site_idSWS_FT_FI4
Number of Residues69
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25961798, ECO:0000269|PubMed:25970245
ChainResidueDetails
AGLY88-LYS107
ALEU297-PRO299
AGLY375-ASP380
APHE471-VAL485
ATHR535-ALA564

site_idSWS_FT_FI5
Number of Residues30
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25961798, ECO:0000269|PubMed:25970245
ChainResidueDetails
AGLY108-SER138

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25961798, ECO:0000269|PubMed:25970245
ChainResidueDetails
ALEU276-TYR296

site_idSWS_FT_FI7
Number of Residues24
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25961798, ECO:0000269|PubMed:25970245
ChainResidueDetails
AASN300-GLY324

site_idSWS_FT_FI8
Number of Residues25
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25970245
ChainResidueDetails
ASER349-LEU374

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25970245
ChainResidueDetails
AVAL381-THR404

site_idSWS_FT_FI10
Number of Residues25
DetailsTRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25970245
ChainResidueDetails
AGLU445-PHE470

site_idSWS_FT_FI11
Number of Residues20
DetailsTRANSMEM: Helical; Name=9 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25970245
ChainResidueDetails
AALA486-ASP506

site_idSWS_FT_FI12
Number of Residues26
DetailsTRANSMEM: Helical; Name=10 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25970245
ChainResidueDetails
AARG508-ILE534

site_idSWS_FT_FI13
Number of Residues22
DetailsTRANSMEM: Helical; Name=11 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25970245
ChainResidueDetails
AGLY565-ARG587

site_idSWS_FT_FI14
Number of Residues20
DetailsTRANSMEM: Helical; Name=12 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25970245
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25970245, ECO:0007744|PDB:4XP1
ChainResidueDetails
AGLY42
AALA44
AVAL45
AASN49
AGLY360
AVAL392
AVAL457
ALEU460
AALA461

site_idSWS_FT_FI16
Number of Residues3
DetailsBINDING: BINDING => ECO:0007744|PDB:4XP1
ChainResidueDetails
AASP46
AALA117
AGLY121

site_idSWS_FT_FI17
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; atypical => ECO:0000269|PubMed:25970245, ECO:0007744|PDB:4XP1
ChainResidueDetails
AASN141

site_idSWS_FT_FI18
Number of Residues7
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AHIS204
ASER213
AGLU222
AGLY228
AGLY233
AVAL264
AASN340

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PDB entries from 2024-11-06

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