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8JXS

Structure of nanobody-bound DRD1_PF-6142 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004952molecular_functiondopamine neurotransmitter receptor activity
A0005886cellular_componentplasma membrane
A0007186biological_processG protein-coupled receptor signaling pathway
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
A0042311biological_processvasodilation
C0005515molecular_functionprotein binding
C0005618cellular_componentcell wall
C0006974biological_processDNA damage response
C0008643biological_processcarbohydrate transport
C0015144molecular_functioncarbohydrate transmembrane transporter activity
C0015768biological_processmaltose transport
C0016020cellular_componentmembrane
C0019865molecular_functionimmunoglobulin binding
C0030288cellular_componentouter membrane-bounded periplasmic space
C0034219biological_processcarbohydrate transmembrane transport
C0034289biological_processdetection of maltose stimulus
C0042597cellular_componentperiplasmic space
C0042956biological_processmaltodextrin transmembrane transport
C0043190cellular_componentATP-binding cassette (ABC) transporter complex
C0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
C0055085biological_processtransmembrane transport
C0060326biological_processcell chemotaxis
C1901982molecular_functionmaltose binding
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIwNLCVISVDRYWaI
ChainResidueDetails
AALA109-ILE125

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
LTYR197-HIS203
HTYR204-HIS210

site_idPS01037
Number of Residues18
DetailsSBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN
ChainResidueDetails
CPRO108-ASN125

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues28
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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