Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3D7M

Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0001664molecular_functionG protein-coupled receptor binding
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005834cellular_componentheterotrimeric G-protein complex
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005938cellular_componentcell cortex
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
A0019001molecular_functionguanyl nucleotide binding
A0019003molecular_functionGDP binding
A0030496cellular_componentmidbody
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
A0031749molecular_functionD2 dopamine receptor binding
A0031821molecular_functionG protein-coupled serotonin receptor binding
A0032794molecular_functionGTPase activating protein binding
A0032991cellular_componentprotein-containing complex
A0043949biological_processregulation of cAMP-mediated signaling
A0046872molecular_functionmetal ion binding
A0050805biological_processnegative regulation of synaptic transmission
A0051301biological_processcell division
A0060236biological_processregulation of mitotic spindle organization
A0098794cellular_componentpostsynapse
A0098978cellular_componentglutamatergic synapse
A0099645biological_processneurotransmitter receptor localization to postsynaptic specialization membrane
A1904322biological_processcellular response to forskolin
A1904778biological_processpositive regulation of protein localization to cell cortex
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 356
ChainResidue
ASER47
ATHR181
AHOH412

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ALF A 357
ChainResidue
ATHR181
AGLY202
AGLY203
AGLN204
AALA41
AGLY42
AGLU43
ALYS46
AARG178
ALYS180

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP A 355
ChainResidue
AGLU43
ASER44
AGLY45
ALYS46
ASER47
ATHR48
AASP150
ASER151
ALEU175
AARG176
ATHR177
AARG178
AASN269
ALYS270
AASP272
ALEU273
ACYS325
AALA326
AHOH403
AHOH404
AHOH412

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:1AS0, ECO:0007744|PDB:1BH2, ECO:0007744|PDB:1GIA, ECO:0007744|PDB:1GIL, ECO:0007744|PDB:3FFA, ECO:0007744|PDB:4N0D, ECO:0007744|PDB:4PAO, ECO:0007744|PDB:4PAQ
ChainResidueDetails
AGLU43
ALEU175
AASP200
AASN269

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:25037222, ECO:0000269|PubMed:9705312, ECO:0007744|PDB:1BH2, ECO:0007744|PDB:4PAO
ChainResidueDetails
ASER47

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:1AS0, ECO:0007744|PDB:1BH2, ECO:0007744|PDB:1GIL, ECO:0007744|PDB:4N0D
ChainResidueDetails
AASP150

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:19703466, ECO:0000269|PubMed:25037222, ECO:0000269|PubMed:9705312, ECO:0007744|PDB:1BH2, ECO:0007744|PDB:4PAO
ChainResidueDetails
ATHR181

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:1AS0, ECO:0007744|PDB:1GIA, ECO:0007744|PDB:1GIL, ECO:0007744|PDB:3FFA, ECO:0007744|PDB:4N0D, ECO:0007744|PDB:4PAO, ECO:0007744|PDB:4PAQ
ChainResidueDetails
AALA326

site_idSWS_FT_FI6
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:26253820
ChainResidueDetails
AGLY2

site_idSWS_FT_FI7
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:26253820
ChainResidueDetails
ACYS3

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
ATHR181
AGLN204
AGLU43
AARG178

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AGLN204

site_idMCSA1
Number of Residues5
DetailsM-CSA 533
ChainResidueDetails
AGLU43electrostatic stabiliser
ATHR48electrostatic stabiliser
AARG178electrostatic stabiliser
AASP200electrostatic stabiliser
AGLN204electrostatic stabiliser

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon