Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8Y2F

Cryo-EM structure of human dopamine transporter in complex with GBR12909

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001504	biological_process	neurotransmitter uptake
A	0002020	molecular_function	protease binding
A	0005102	molecular_function	signaling receptor binding
A	0005326	molecular_function	neurotransmitter transmembrane transporter activity
A	0005330	molecular_function	dopamine:sodium symporter activity
A	0005334	molecular_function	norepinephrine:sodium symporter activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005886	cellular_component	plasma membrane
A	0006836	biological_process	neurotransmitter transport
A	0006865	biological_process	amino acid transport
A	0007595	biological_process	lactation
A	0007608	biological_process	sensory perception of smell
A	0007626	biological_process	locomotory behavior
A	0008504	molecular_function	monoamine transmembrane transporter activity
A	0009410	biological_process	response to xenobiotic stimulus
A	0009986	cellular_component	cell surface
A	0010039	biological_process	response to iron ion
A	0015293	molecular_function	symporter activity
A	0015844	biological_process	monoamine transport
A	0015872	biological_process	dopamine transport
A	0016020	cellular_component	membrane
A	0016600	cellular_component	flotillin complex
A	0021984	biological_process	adenohypophysis development
A	0022857	molecular_function	transmembrane transporter activity
A	0030424	cellular_component	axon
A	0035094	biological_process	response to nicotine
A	0035240	molecular_function	dopamine binding
A	0035725	biological_process	sodium ion transmembrane transport
A	0040018	biological_process	positive regulation of multicellular organism growth
A	0042053	biological_process	regulation of dopamine metabolic process
A	0042220	biological_process	response to cocaine
A	0042416	biological_process	dopamine biosynthetic process
A	0042420	biological_process	dopamine catabolic process
A	0042734	cellular_component	presynaptic membrane
A	0042995	cellular_component	cell projection
A	0043005	cellular_component	neuron projection
A	0043025	cellular_component	neuronal cell body
A	0043176	molecular_function	amine binding
A	0043679	cellular_component	axon terminus
A	0044877	molecular_function	protein-containing complex binding
A	0045121	cellular_component	membrane raft
A	0045211	cellular_component	postsynaptic membrane
A	0045471	biological_process	response to ethanol
A	0046872	molecular_function	metal ion binding
A	0050890	biological_process	cognition
A	0051583	biological_process	dopamine uptake involved in synaptic transmission
A	0051591	biological_process	response to cAMP
A	0051620	biological_process	norepinephrine uptake
A	0051721	molecular_function	protein phosphatase 2A binding
A	0060134	biological_process	prepulse inhibition
A	0090494	biological_process	dopamine uptake
A	0098691	cellular_component	dopaminergic synapse
A	1901363	molecular_function	heterocyclic compound binding
A	1990384	biological_process	hyaloid vascular plexus regression

Functional Information from PROSITE/UniProt

site_id	PS00610
Number of Residues	15
Details	NA_NEUROTRAN_SYMP_1 Sodium:neurotransmitter symporter family signature 1. WRFPYlcykNGGGaF

Chain	Residue	Details
A	TRP84-PHE98

site_id	PS00754
Number of Residues	21
Details	NA_NEUROTRAN_SYMP_2 Sodium:neurotransmitter symporter family signature 2. YLfsSFTteLPWihCnnswNS

Chain	Residue	Details
A	TYR166-SER186

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	31
Details	TRANSMEM: Helical; Name=2 => ECO:0000269\|PubMed:39112701, ECO:0000269\|PubMed:39112703, ECO:0000269\|PubMed:39112705, ECO:0007744\|PDB:8VBY, ECO:0007744\|PDB:8Y2C, ECO:0007744\|PDB:8Y2D, ECO:0007744\|PDB:8Y2E, ECO:0007744\|PDB:8Y2F, ECO:0007744\|PDB:8Y2G, ECO:0007744\|PDB:9EO4

Chain	Residue	Details
A	GLY96-GLY127

site_id	SWS_FT_FI2
Number of Residues	43
Details	TRANSMEM: Helical; Name=3 => ECO:0000269\|PubMed:39112701, ECO:0000269\|PubMed:39112703, ECO:0000269\|PubMed:39112705, ECO:0007744\|PDB:8VBY, ECO:0007744\|PDB:8Y2C, ECO:0007744\|PDB:8Y2D, ECO:0007744\|PDB:8Y2E, ECO:0007744\|PDB:8Y2F, ECO:0007744\|PDB:8Y2G, ECO:0007744\|PDB:9EO4

Chain	Residue	Details
A	ALA128-PHE171

site_id	SWS_FT_FI3
Number of Residues	115
Details	TOPO_DOM: Extracellular => ECO:0000269\|PubMed:39112701, ECO:0000269\|PubMed:39112703, ECO:0000269\|PubMed:39112705, ECO:0007744\|PDB:8VBY, ECO:0007744\|PDB:8Y2C, ECO:0007744\|PDB:8Y2D, ECO:0007744\|PDB:8Y2E, ECO:0007744\|PDB:8Y2F, ECO:0007744\|PDB:8Y2G, ECO:0007744\|PDB:9EO4

Chain	Residue	Details
A	THR172-PRO236
A	PRO288-CYS306
A	VAL377-THR400
A	PHE543-PHE553

site_id	SWS_FT_FI4
Number of Residues	19
Details	TRANSMEM: Helical; Name=4 => ECO:0000269\|PubMed:39112701, ECO:0000269\|PubMed:39112703, ECO:0000269\|PubMed:39112705, ECO:0007744\|PDB:8VBY, ECO:0007744\|PDB:8Y2C, ECO:0007744\|PDB:8Y2D, ECO:0007744\|PDB:8Y2E, ECO:0007744\|PDB:8Y2F, ECO:0007744\|PDB:8Y2G, ECO:0007744\|PDB:9EO4

Chain	Residue	Details
A	ARG237-TRP256

site_id	SWS_FT_FI5
Number of Residues	30
Details	TRANSMEM: Helical; Name=5 => ECO:0000269\|PubMed:39112701, ECO:0000269\|PubMed:39112703, ECO:0000269\|PubMed:39112705, ECO:0007744\|PDB:8VBY, ECO:0007744\|PDB:8Y2C, ECO:0007744\|PDB:8Y2D, ECO:0007744\|PDB:8Y2E, ECO:0007744\|PDB:8Y2F, ECO:0007744\|PDB:8Y2G, ECO:0007744\|PDB:9EO4

Chain	Residue	Details
A	LYS257-LEU287

site_id	SWS_FT_FI6
Number of Residues	28
Details	TRANSMEM: Discontinuously helical; Name=6 => ECO:0000269\|PubMed:39112701, ECO:0000269\|PubMed:39112703, ECO:0000269\|PubMed:39112705, ECO:0007744\|PDB:8VBY, ECO:0007744\|PDB:8Y2C, ECO:0007744\|PDB:8Y2D, ECO:0007744\|PDB:8Y2E, ECO:0007744\|PDB:8Y2F, ECO:0007744\|PDB:8Y2G, ECO:0007744\|PDB:9EO4

Chain	Residue	Details
A	GLU307-TYR335

site_id	SWS_FT_FI7
Number of Residues	40
Details	TRANSMEM: Helical; Name=7 => ECO:0000269\|PubMed:39112701, ECO:0000269\|PubMed:39112703, ECO:0000269\|PubMed:39112705, ECO:0007744\|PDB:8VBY, ECO:0007744\|PDB:8Y2C, ECO:0007744\|PDB:8Y2D, ECO:0007744\|PDB:8Y2E, ECO:0007744\|PDB:8Y2F, ECO:0007744\|PDB:8Y2G, ECO:0007744\|PDB:9EO4

Chain	Residue	Details
A	ASN336-SER376

site_id	SWS_FT_FI8
Number of Residues	41
Details	TRANSMEM: Helical; Name=8 => ECO:0000269\|PubMed:39112701, ECO:0000269\|PubMed:39112703, ECO:0000269\|PubMed:39112705, ECO:0007744\|PDB:8VBY, ECO:0007744\|PDB:8Y2C, ECO:0007744\|PDB:8Y2D, ECO:0007744\|PDB:8Y2E, ECO:0007744\|PDB:8Y2F, ECO:0007744\|PDB:8Y2G, ECO:0007744\|PDB:9EO4

Chain	Residue	Details
A	LEU401-HIS442

site_id	SWS_FT_FI9
Number of Residues	23
Details	TRANSMEM: Helical; Name=9 => ECO:0000269\|PubMed:39112701, ECO:0000269\|PubMed:39112703, ECO:0000269\|PubMed:39112705, ECO:0007744\|PDB:8VBY, ECO:0007744\|PDB:8Y2C, ECO:0007744\|PDB:8Y2D, ECO:0007744\|PDB:8Y2E, ECO:0007744\|PDB:8Y2F, ECO:0007744\|PDB:8Y2G, ECO:0007744\|PDB:9EO4

Chain	Residue	Details
A	ARG443-ASN466

site_id	SWS_FT_FI10
Number of Residues	32
Details	TRANSMEM: Helical; Name=10 => ECO:0000269\|PubMed:39112701, ECO:0000269\|PubMed:39112703, ECO:0000269\|PubMed:39112705, ECO:0007744\|PDB:8VBY, ECO:0007744\|PDB:8Y2C, ECO:0007744\|PDB:8Y2D, ECO:0007744\|PDB:8Y2E, ECO:0007744\|PDB:8Y2F, ECO:0007744\|PDB:8Y2G, ECO:0007744\|PDB:9EO4

Chain	Residue	Details
A	GLY467-TYR499

site_id	SWS_FT_FI11
Number of Residues	52
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:39112701, ECO:0000269\|PubMed:39112703, ECO:0000269\|PubMed:39112705, ECO:0007744\|PDB:8VBY, ECO:0007744\|PDB:8Y2C, ECO:0007744\|PDB:8Y2D, ECO:0007744\|PDB:8Y2E, ECO:0007744\|PDB:8Y2F, ECO:0007744\|PDB:8Y2G, ECO:0007744\|PDB:9EO4

Chain	Residue	Details
A	GLY500-PRO516
A	PRO584-VAL620

site_id	SWS_FT_FI12
Number of Residues	25
Details	TRANSMEM: Helical; Name=11 => ECO:0000269\|PubMed:39112701, ECO:0000269\|PubMed:39112703, ECO:0000269\|PubMed:39112705, ECO:0007744\|PDB:8VBY, ECO:0007744\|PDB:8Y2C, ECO:0007744\|PDB:8Y2D, ECO:0007744\|PDB:8Y2E, ECO:0007744\|PDB:8Y2F, ECO:0007744\|PDB:8Y2G, ECO:0007744\|PDB:9EO4

Chain	Residue	Details
A	SER517-THR542

site_id	SWS_FT_FI13
Number of Residues	29
Details	TRANSMEM: Helical; Name=12 => ECO:0000269\|PubMed:39112701, ECO:0000269\|PubMed:39112703, ECO:0000269\|PubMed:39112705, ECO:0007744\|PDB:8VBY, ECO:0007744\|PDB:8Y2C, ECO:0007744\|PDB:8Y2D, ECO:0007744\|PDB:8Y2E, ECO:0007744\|PDB:8Y2F, ECO:0007744\|PDB:8Y2G, ECO:0007744\|PDB:9EO4

Chain	Residue	Details
A	PRO554-LEU583

site_id	SWS_FT_FI14
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:39112703, ECO:0000269\|PubMed:39112705, ECO:0007744\|PDB:8VBY, ECO:0007744\|PDB:9EO4

Chain	Residue	Details
A	GLY75
A	VAL78
A	LEU418
A	ASP421
A	SER422

site_id	SWS_FT_FI15
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:39112701, ECO:0007744\|PDB:8Y2D, ECO:0007744\|PDB:8Y2G

Chain	Residue	Details
A	ALA77
A	ASP79
A	ASN82
A	SER321
A	ASN353

site_id	SWS_FT_FI16
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:39112701, ECO:0007744\|PDB:8Y2D

Chain	Residue	Details
A	SER149
A	GLY153
A	PHE320
A	ALA423

site_id	SWS_FT_FI17
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:39112701, ECO:0000269\|PubMed:39112703, ECO:0007744\|PDB:8Y2D, ECO:0007744\|PDB:8Y2G, ECO:0007744\|PDB:9EO4

Chain	Residue	Details
A	GLN317
A	SER357

site_id	SWS_FT_FI18
Number of Residues	1
Details	SITE: Contributes to high-affinity binding to cocaine => ECO:0000250\|UniProtKB:Q61327

Chain	Residue	Details
A	PHE105

site_id	SWS_FT_FI19
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:39112701, ECO:0007744\|PDB:8Y2C, ECO:0007744\|PDB:8Y2E, ECO:0007744\|PDB:8Y2F, ECO:0007744\|PDB:8Y2G

Chain	Residue	Details
A	ASN181
A	ASN188

site_id	SWS_FT_FI20
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN205

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		Validation report (PDF)