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6IQL

Crystal structure of dopamine receptor D4 bound to the subtype-selective ligand, L745870

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004952molecular_functiondopamine neurotransmitter receptor activity
A0005506molecular_functioniron ion binding
A0005886cellular_componentplasma membrane
A0007186biological_processG protein-coupled receptor signaling pathway
A0007195biological_processadenylate cyclase-inhibiting dopamine receptor signaling pathway
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0004930molecular_functionG protein-coupled receptor activity
B0004952molecular_functiondopamine neurotransmitter receptor activity
B0005506molecular_functioniron ion binding
B0005886cellular_componentplasma membrane
B0007186biological_processG protein-coupled receptor signaling pathway
B0007195biological_processadenylate cyclase-inhibiting dopamine receptor signaling pathway
B0009055molecular_functionelectron transfer activity
B0016020cellular_componentmembrane
B0020037molecular_functionheme binding
B0022900biological_processelectron transport chain
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue L74 A 1201
ChainResidue
APHE88
ATYR358
ASER91
AGLY96
ATRP98
AMET109
AASP112
AVAL113
APHE330
APHE331

site_idAC2
Number of Residues9
Detailsbinding site for residue L74 B 1201
ChainResidue
BPHE88
BSER91
BGLY96
BTRP98
BASP112
BVAL113
BCYS180
BPHE330
BTYR358

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIwNLCAISVDRFVaV
ChainResidueDetails
AALA118-VAL134

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues44
DetailsTRANSMEM: Helical; Name=1 => ECO:0000250|UniProtKB:P21917
ChainResidueDetails
ALEU35-ALA57
BLEU35-ALA57

site_idSWS_FT_FI2
Number of Residues86
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:P21917
ChainResidueDetails
ASER58-ASN67
AASP129-CYS146
AILE370-CYS387
BSER58-ASN67
BASP129-CYS146
BILE370-CYS387

site_idSWS_FT_FI3
Number of Residues44
DetailsTRANSMEM: Helical; Name=2 => ECO:0000250|UniProtKB:P21917
ChainResidueDetails
ATYR68-TYR90
BTYR68-TYR90

site_idSWS_FT_FI4
Number of Residues76
DetailsTOPO_DOM: Extracellular => ECO:0000250|UniProtKB:P21917
ChainResidueDetails
ASER91-ASP106
AASP171-ASP186
AALA338-SER346
BSER91-ASP106
BASP171-ASP186
BALA338-SER346

site_idSWS_FT_FI5
Number of Residues42
DetailsTRANSMEM: Helical; Name=3 => ECO:0000250|UniProtKB:P21917
ChainResidueDetails
ATHR107-VAL128
BTHR107-VAL128

site_idSWS_FT_FI6
Number of Residues46
DetailsTRANSMEM: Helical; Name=4 => ECO:0000250|UniProtKB:P21917
ChainResidueDetails
AGLN147-ASN170
BGLN147-ASN170

site_idSWS_FT_FI7
Number of Residues42
DetailsTRANSMEM: Helical; Name=5 => ECO:0000250|UniProtKB:P21917
ChainResidueDetails
ATYR187-TRP208
BTYR187-TRP208

site_idSWS_FT_FI8
Number of Residues44
DetailsTRANSMEM: Helical; Name=6 => ECO:0000250|UniProtKB:P21917
ChainResidueDetails
AVAL315-ARG337
BVAL315-ARG337

site_idSWS_FT_FI9
Number of Residues44
DetailsTRANSMEM: Helical; Name=7 => ECO:0000250|UniProtKB:P21917
ChainResidueDetails
APRO347-THR369
BPRO347-THR369

site_idSWS_FT_FI10
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P21917
ChainResidueDetails
AASP77
ASER119
BASP77
BSER119

site_idSWS_FT_FI11
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P21917
ChainResidueDetails
ACYS387
BCYS387

site_idSWS_FT_FI12
Number of Residues4
DetailsBINDING: axial binding residue
ChainResidueDetails
ATRP1007
AILE1102
BTRP1007
BILE1102

223790

PDB entries from 2024-08-14

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