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8WCC

Cryo-EM structure of the CHA-bound mTAAR1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
R0001594molecular_functiontrace-amine receptor activity
R0004930molecular_functionG protein-coupled receptor activity
R0005783cellular_componentendoplasmic reticulum
R0005789cellular_componentendoplasmic reticulum membrane
R0005886cellular_componentplasma membrane
R0007186biological_processG protein-coupled receptor signaling pathway
R0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
R0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
R0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
R0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
R0008227molecular_functionG protein-coupled amine receptor activity
R0012505cellular_componentendomembrane system
R0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIfHLAFISIDRYCaV
ChainResidueDetails
RALA108-VAL124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues60
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465
ChainResidueDetails
RMET1-ALA23
RGLU161-LYS187
RASP271-ASN283

site_idSWS_FT_FI2
Number of Residues24
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465
ChainResidueDetails
RSER24-SER48

site_idSWS_FT_FI3
Number of Residues90
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465
ChainResidueDetails
RHIS49-ASN58
RASP119-THR138
RARG211-ALA246
RTYR305-LEU332

site_idSWS_FT_FI4
Number of Residues21
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465
ChainResidueDetails
RTRP59-MET80

site_idSWS_FT_FI5
Number of Residues14
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465, ECO:0000305
ChainResidueDetails
RVAL81-CYS95

site_idSWS_FT_FI6
Number of Residues22
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465
ChainResidueDetails
RLYS96-ILE118

site_idSWS_FT_FI7
Number of Residues21
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465
ChainResidueDetails
RILE139-LEU160

site_idSWS_FT_FI8
Number of Residues22
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465
ChainResidueDetails
RVAL188-TYR210

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465
ChainResidueDetails
RALA247-LEU270

site_idSWS_FT_FI10
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465
ChainResidueDetails
RASP284-PHE304

site_idSWS_FT_FI11
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:37963465, ECO:0007744|PDB:8WC6
ChainResidueDetails
RASP102

site_idSWS_FT_FI12
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
RASN9

227111

PDB entries from 2024-11-06

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