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9AVL

Structure of human calcium-sensing receptor in complex with Gi3 protein in nanodiscs

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0001664molecular_functionG protein-coupled receptor binding
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0005813cellular_componentcentrosome
A0005834cellular_componentheterotrimeric G-protein complex
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0007165biological_processsignal transduction
A0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
A0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A0007194biological_processnegative regulation of adenylate cyclase activity
A0007212biological_processG protein-coupled dopamine receptor signaling pathway
A0016020cellular_componentmembrane
A0016239biological_processpositive regulation of macroautophagy
A0019003molecular_functionGDP binding
A0030496cellular_componentmidbody
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
A0046039biological_processGTP metabolic process
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
A0070062cellular_componentextracellular exosome
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005765cellular_componentlysosomal membrane
B0005829cellular_componentcytosol
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
B0005925cellular_componentfocal adhesion
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0016020cellular_componentmembrane
B0030159molecular_functionsignaling receptor complex adaptor activity
B0031982cellular_componentvesicle
B0044877molecular_functionprotein-containing complex binding
B0048471cellular_componentperinuclear region of cytoplasm
B0051020molecular_functionGTPase binding
B0070062cellular_componentextracellular exosome
B1901379biological_processregulation of potassium ion transmembrane transport
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
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299

site_idPS00979
Number of Residues19
DetailsG_PROTEIN_RECEP_F3_1 G-protein coupled receptors family 3 signature 1. VaNLLgLFyIPQVSyASSS
ChainResidueDetails
QVAL153-SER171

site_idPS00980
Number of Residues25
DetailsG_PROTEIN_RECEP_F3_2 G-protein coupled receptors family 3 signature 2. CCFeCveCpdgeYsdet.DasACnkC
ChainResidueDetails
QCYS561-CYS585

site_idPS00981
Number of Residues11
DetailsG_PROTEIN_RECEP_F3_3 G-protein coupled receptors family 3 signature 3. FNEAKfITFSM
ChainResidueDetails
QPHE801-MET811

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378
ChainResidueDetails
GALA2
ALEU175
AASN269
QTYR829-VAL836
RTYR20-PHE612
RGLU671-GLN681
RALA746-SER769
RTYR829-VAL836

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Cysteine methyl ester => ECO:0000250|UniProtKB:P63212
ChainResidueDetails
GCYS68
ATHR181

site_idSWS_FT_FI3
Number of Residues1
DetailsLIPID: S-geranylgeranyl cysteine => ECO:0000250|UniProtKB:P63212
ChainResidueDetails
GCYS68
QARG701-GLN724
QLYS793-LYS805
RLYS636-GLU649
RARG701-GLN724
RLYS793-LYS805

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:19478087, ECO:0007744|PDB:2V4Z
ChainResidueDetails
AASP200
RLEU650-GLY670

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:2IHB, ECO:0007744|PDB:2ODE, ECO:0007744|PDB:2V4Z, ECO:0007744|PDB:4G5O, ECO:0007744|PDB:4G5R
ChainResidueDetails
ASER326
RPRO682-ASN700

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250
ChainResidueDetails
AARG178
RPHE725-THR745

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269|PubMed:24141704
ChainResidueDetails
AGLN204
RLEU770-PHE792

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: ADP-ribosylcysteine; by pertussis toxin => ECO:0000250
ChainResidueDetails
ACYS351
RPHE806-THR828

site_idSWS_FT_FI9
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:25255805
ChainResidueDetails
AGLY2
RGLU837-PHE862

site_idSWS_FT_FI10
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250
ChainResidueDetails
ACYS3
RASP234
RARG415
RGLY557
QTHR145
QGLU231
QASP234
QARG415
QGLY557
RARG66
RTHR145
RGLU231

site_idSWS_FT_FI11
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:27434672, ECO:0000305|PubMed:27386547, ECO:0007744|PDB:5FBH, ECO:0007744|PDB:5FBK, ECO:0007744|PDB:5K5S
ChainResidueDetails
QILE81
QLEU87
QLEU88
RILE81
RLEU87
RLEU88

site_idSWS_FT_FI12
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:27434672, ECO:0000305|PubMed:27386547, ECO:0007744|PDB:5FBK, ECO:0007744|PDB:5K5S
ChainResidueDetails
QSER84
RSER84

site_idSWS_FT_FI13
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:27434672, ECO:0007744|PDB:5K5S, ECO:0007744|PDB:5K5T
ChainResidueDetails
QTHR100
RTHR100

site_idSWS_FT_FI14
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:27386547, ECO:0000269|PubMed:27434672, ECO:0007744|PDB:5FBH, ECO:0007744|PDB:5FBK, ECO:0007744|PDB:5K5S
ChainResidueDetails
QSER147
QALA168
QSER170
QGLU297
RSER147
RALA168
RSER170
RGLU297

site_idSWS_FT_FI15
Number of Residues2
DetailsSITE: Important for ability of agonist AMG 416 to activate G-protein-coupled receptor activity => ECO:0000269|PubMed:26290606
ChainResidueDetails
QCYS482
RCYS482

site_idSWS_FT_FI16
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
QASN90
QASN130
QASN386
QASN400
RASN90
RASN130
RASN386
RASN400

site_idSWS_FT_FI17
Number of Residues14
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:27434672
ChainResidueDetails
QASN261
RASN446
RASN468
RASN488
RASN541
RASN594
QASN287
QASN446
QASN468
QASN488
QASN541
QASN594
RASN261
RASN287

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PDB entries from 2024-07-24

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