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6ZIZ

CRYSTAL STRUCTURE OF NRAS Q61R IN COMPLEX WITH GTP AND COMPOUND 18

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000165biological_processMAPK cascade
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
A0045445biological_processmyoblast differentiation
A0070062cellular_componentextracellular exosome
A0070821cellular_componenttertiary granule membrane
B0000139cellular_componentGolgi membrane
B0000165biological_processMAPK cascade
B0001938biological_processpositive regulation of endothelial cell proliferation
B0003924molecular_functionGTPase activity
B0003925molecular_functionG protein activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005789cellular_componentendoplasmic reticulum membrane
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007265biological_processRas protein signal transduction
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0019003molecular_functionGDP binding
B0044877molecular_functionprotein-containing complex binding
B0045445biological_processmyoblast differentiation
B0070062cellular_componentextracellular exosome
B0070821cellular_componenttertiary granule membrane
Functional Information from PDB Data
site_idAC1
Number of Residues27
Detailsbinding site for residue GTP A 201
ChainResidue
AGLY12
AASP30
ATYR32
APRO34
ATHR35
AGLY60
AASN116
ALYS117
AASP119
ALEU120
ASER145
AGLY13
AALA146
AMG202
AHOH316
AHOH320
AHOH325
AHOH338
AHOH347
AHOH380
AVAL14
AGLY15
ALYS16
ASER17
AALA18
APHE28
AVAL29

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 202
ChainResidue
ASER17
ATHR35
AGTP201
AHOH320
AHOH325

site_idAC3
Number of Residues9
Detailsbinding site for residue EZZ A 203
ChainResidue
ALYS5
AVAL7
AGLU37
AASP54
ALEU56
AARG73
ATHR74
AGLY75
AHOH379

site_idAC4
Number of Residues25
Detailsbinding site for residue GTP B 201
ChainResidue
BGLY12
BGLY13
BVAL14
BGLY15
BLYS16
BSER17
BALA18
BPHE28
BVAL29
BASP30
BTYR32
BPRO34
BTHR35
BGLY60
BASN116
BLYS117
BASP119
BLEU120
BSER145
BALA146
BMG202
BHOH317
BHOH320
BHOH339
BHOH341

site_idAC5
Number of Residues5
Detailsbinding site for residue MG B 202
ChainResidue
BSER17
BTHR35
BGTP201
BHOH306
BHOH317

site_idAC6
Number of Residues8
Detailsbinding site for residue EZZ B 203
ChainResidue
BLYS5
BVAL7
BGLU37
BASP54
BLEU56
BTYR71
BTHR74
BGLY75

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|Ref.25
ChainResidueDetails
AGLY10
AVAL29
AASN116
BGLY10
BVAL29
BASN116

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AASP57
BASP57

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by STK19 => ECO:0000269|PubMed:30712867
ChainResidueDetails
ASER89
BSER89

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: (Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL => ECO:0000269|PubMed:19744486
ChainResidueDetails
ATHR35
BTHR35

site_idSWS_FT_FI5
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:30442762
ChainResidueDetails
ALYS170
BLYS170

219140

PDB entries from 2024-05-01

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