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6K41

cryo-EM structure of alpha2BAR-GoA complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005834cellular_componentheterotrimeric G-protein complex
A0005886cellular_componentplasma membrane
A0006904biological_processvesicle docking involved in exocytosis
A0006936biological_processmuscle contraction
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
A0007212biological_processG protein-coupled dopamine receptor signaling pathway
A0007626biological_processlocomotory behavior
A0008016biological_processregulation of heart contraction
A0016020cellular_componentmembrane
A0019001molecular_functionguanyl nucleotide binding
A0030425cellular_componentdendrite
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
A0031821molecular_functionG protein-coupled serotonin receptor binding
A0031852molecular_functionmu-type opioid receptor binding
A0044297cellular_componentcell body
A0046676biological_processnegative regulation of insulin secretion
A0046872molecular_functionmetal ion binding
A0051430molecular_functioncorticotropin-releasing hormone receptor 1 binding
B0001750cellular_componentphotoreceptor outer segment
B0001917cellular_componentphotoreceptor inner segment
B0003924molecular_functionGTPase activity
B0005737cellular_componentcytoplasm
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
B0007204biological_processpositive regulation of cytosolic calcium ion concentration
B0007603biological_processphototransduction, visible light
B0008283biological_processcell population proliferation
B0010659biological_processcardiac muscle cell apoptotic process
B0030159molecular_functionsignaling receptor complex adaptor activity
B0030425cellular_componentdendrite
B0030507molecular_functionspectrin binding
B0042622cellular_componentphotoreceptor outer segment membrane
B0043209cellular_componentmyelin sheath
B0044297cellular_componentcell body
B0044877molecular_functionprotein-containing complex binding
B0045202cellular_componentsynapse
B0047391molecular_functionalkylglycerophosphoethanolamine phosphodiesterase activity
B0050909biological_processsensory perception of taste
B0051020molecular_functionGTPase binding
B0060041biological_processretina development in camera-type eye
B0071456biological_processcellular response to hypoxia
G0005515molecular_functionprotein binding
G0005834cellular_componentheterotrimeric G-protein complex
G0005886cellular_componentplasma membrane
G0007165biological_processsignal transduction
G0007186biological_processG protein-coupled receptor signaling pathway
G0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
G0016020cellular_componentmembrane
G0031681molecular_functionG-protein beta-subunit binding
G0048144biological_processfibroblast proliferation
G0070062cellular_componentextracellular exosome
G0071380biological_processcellular response to prostaglandin E stimulus
G0071870biological_processcellular response to catecholamine stimulus
R0003796molecular_functionlysozyme activity
R0004930molecular_functionG protein-coupled receptor activity
R0007186biological_processG protein-coupled receptor signaling pathway
R0009253biological_processpeptidoglycan catabolic process
R0016020cellular_componentmembrane
R0016998biological_processcell wall macromolecule catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue CZX R 501
ChainResidue
RASP92
RCYS96
RTHR97
RSER176
RSER180
RPHE387
RPHE388
RPHE412

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. SSIvHLCAISLDRYWaV
ChainResidueDetails
RSER98-VAL114

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
RALA-163
ASER47
ALEU176
ATHR182
AASP201
AASN270
AALA326

site_idSWS_FT_FI2
Number of Residues25
DetailsTRANSMEM: Helical; Name=1 => ECO:0000250
ChainResidueDetails
RALA13-LEU38

site_idSWS_FT_FI3
Number of Residues226
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250
ChainResidueDetails
RTHR39-ASN48
RLEU108-ARG128
RTHR427-TRP450

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000250
ChainResidueDetails
RLEU49-SER69

site_idSWS_FT_FI5
Number of Residues53
DetailsTOPO_DOM: Extracellular => ECO:0000250
ChainResidueDetails
RLEU70-GLU86
RTYR150-TYR172
RSER390-HIS405

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000250
ChainResidueDetails
RVAL87-SER107

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000250
ChainResidueDetails
RILE129-ILE149

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000250
ChainResidueDetails
RILE173-LEU193

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000250
ChainResidueDetails
RPHE369-PHE389

site_idSWS_FT_FI10
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000250
ChainResidueDetails
RGLY406-TYR426

site_idSWS_FT_FI11
Number of Residues1
DetailsSITE: Implicated in ligand binding => ECO:0000250
ChainResidueDetails
RASP92

site_idSWS_FT_FI12
Number of Residues2
DetailsSITE: Implicated in catechol agonist binding => ECO:0000250
ChainResidueDetails
RSER176
RSER180

site_idSWS_FT_FI13
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000255
ChainResidueDetails
RCYS442

222624

PDB entries from 2024-07-17

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