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4DSU

Small-molecule ligands bind to a distinct pocket in Ras and inhibit SOS-mediated nucleotide exchange activity

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000165biological_processMAPK cascade
A0000166molecular_functionnucleotide binding
A0001889biological_processliver development
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005741cellular_componentmitochondrial outer membrane
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0007165biological_processsignal transduction
A0007265biological_processRas protein signal transduction
A0007565biological_processfemale pregnancy
A0008283biological_processcell population proliferation
A0008542biological_processvisual learning
A0009629biological_processresponse to gravity
A0009898cellular_componentcytoplasmic side of plasma membrane
A0010467biological_processgene expression
A0010628biological_processpositive regulation of gene expression
A0012505cellular_componentendomembrane system
A0014009biological_processglial cell proliferation
A0016020cellular_componentmembrane
A0016601biological_processRac protein signal transduction
A0016787molecular_functionhydrolase activity
A0019002molecular_functionGMP binding
A0019003molecular_functionGDP binding
A0019221biological_processcytokine-mediated signaling pathway
A0021897biological_processforebrain astrocyte development
A0030036biological_processactin cytoskeleton organization
A0030275molecular_functionLRR domain binding
A0030857biological_processnegative regulation of epithelial cell differentiation
A0032228biological_processregulation of synaptic transmission, GABAergic
A0035022biological_processpositive regulation of Rac protein signal transduction
A0035900biological_processresponse to isolation stress
A0035914biological_processskeletal muscle cell differentiation
A0043495molecular_functionmembrane-membrane adaptor activity
A0043524biological_processnegative regulation of neuron apoptotic process
A0044877molecular_functionprotein-containing complex binding
A0048169biological_processregulation of long-term neuronal synaptic plasticity
A0048873biological_processhomeostasis of number of cells within a tissue
A0051146biological_processstriated muscle cell differentiation
A0051384biological_processresponse to glucocorticoid
A0051385biological_processresponse to mineralocorticoid
A0051402biological_processneuron apoptotic process
A0051450biological_processmyoblast proliferation
A0060038biological_processcardiac muscle cell proliferation
A0060252biological_processpositive regulation of glial cell proliferation
A0060441biological_processepithelial tube branching involved in lung morphogenesis
A0060509biological_processtype I pneumocyte differentiation
A2000774biological_processpositive regulation of cellular senescence
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE GDP A 201
ChainResidue
AGLY13
AGLU31
AASN116
ALYS117
AASP119
ALEU120
ASER145
AALA146
ALYS147
AMG202
AHOH305
AVAL14
AHOH308
AHOH323
AHOH327
AHOH332
AHOH346
AGLY15
ALYS16
ASER17
AALA18
APHE28
AVAL29
AASP30

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 202
ChainResidue
ASER17
AGDP201
AHOH304
AHOH305
AHOH309
AHOH346

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BZI A 203
ChainResidue
ALYS5
ALEU6
AVAL7
AASP54
AHOH361

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:22566140, ECO:0000305|PubMed:34380736, ECO:0000305|PubMed:35522713
ChainResidueDetails
AGLY10
AVAL29
AALA59
AASN116

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylthreonine; in GTPase KRas, N-terminally processed => ECO:0000269|Ref.17
ChainResidueDetails
ATHR2

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:22711838
ChainResidueDetails
ALYS104

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Cysteine methyl ester => ECO:0000269|PubMed:27791178, ECO:0007744|PDB:5TAR, ECO:0007744|PDB:5TB5
ChainResidueDetails
AVAL186

site_idSWS_FT_FI5
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000305|PubMed:29239724
ChainResidueDetails
ALYS180

site_idSWS_FT_FI6
Number of Residues1
DetailsLIPID: N6-palmitoyl lysine => ECO:0000269|PubMed:29239724
ChainResidueDetails
ALYS182

site_idSWS_FT_FI7
Number of Residues2
DetailsLIPID: N6-palmitoyl lysine => ECO:0000305|PubMed:29239724
ChainResidueDetails
ALYS184
ACYS185

site_idSWS_FT_FI8
Number of Residues1
DetailsLIPID: S-farnesyl cysteine => ECO:0000269|PubMed:27791178, ECO:0000305|PubMed:24415755, ECO:0007744|PDB:5TAR, ECO:0007744|PDB:5TB5
ChainResidueDetails
AVAL186

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: (Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL => ECO:0000269|PubMed:19744486
ChainResidueDetails
ATHR35

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:30442762
ChainResidueDetails
AMET170

237735

PDB entries from 2025-06-18

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