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3CON

Crystal structure of the human NRAS GTPase bound with GDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000165biological_processMAPK cascade
A0000166molecular_functionnucleotide binding
A0001938biological_processpositive regulation of endothelial cell proliferation
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0007165biological_processsignal transduction
A0007265biological_processRas protein signal transduction
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019003molecular_functionGDP binding
A0044877molecular_functionprotein-containing complex binding
A0070062cellular_componentextracellular exosome
A0070821cellular_componenttertiary granule membrane
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 202
ChainResidue
ASER17
AHOH226
AHOH265
AHOH279
AHOH282

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 203
ChainResidue
AHOH252
AHOH278
AGLY48
AHOH247
AHOH249
AHOH250

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 204
ChainResidue
AASP38
AHOH280
AHOH283
AHOH284
AHOH294

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 205
ChainResidue
AHOH231
AHOH245

site_idAC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE GDP A 201
ChainResidue
AGLY13
AGLY15
ALYS16
ASER17
AALA18
APHE28
AASP30
ATYR32
AASN116
ALYS117
AASP119
ALEU120
ASER145
AALA146
ALYS147
AHOH221
AHOH235
AHOH270
AHOH273
AHOH279
AHOH282
AHOH290
AHOH291

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE UNX A 206
ChainResidue
AASP47
AARG102

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE UNX A 207
ChainResidue
ALEU6
AASP54

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE UNX A 208
ChainResidue
AGLY10
ATHR58
ATYR96
AHOH234
AHOH236

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX A 209
ChainResidue
AGLY10
AALA11
ASER89

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNX A 200
ChainResidue
AGLU31
AARG149
AGLU153
AHOH219

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNX A 211
ChainResidue
ASER87
ALYS88
ATHR124
AHOH217

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX A 212
ChainResidue
AASN94
ALEU95
AHOH233

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE UNX A 213
ChainResidue
AASP154
AARG161

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|Ref.29
ChainResidueDetails
AGLY10
AVAL29
AASN116

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AASP57

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by STK19 => ECO:0000269|PubMed:30712867
ChainResidueDetails
ASER89

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: (Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL => ECO:0000269|PubMed:19744486
ChainResidueDetails
ATHR35

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:30442762
ChainResidueDetails
ALYS170

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PDB entries from 2025-06-18

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