Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4DSN

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 Residues30
DetailsBINDING SITE FOR RESIDUE GCP A 201
ChainResidue
AASP12
AASP30
AGLU31
ATYR32
APRO34
ATHR35
AGLY60
AASN116
ALYS117
AASP119
ALEU120
AGLY13
ASER145
AALA146
ALYS147
AMG202
AHOH301
AHOH302
AHOH303
AHOH309
AHOH319
AHOH333
AVAL14
AHOH336
AGLY15
ALYS16
ASER17
AALA18
APHE28
AVAL29

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 202
ChainResidue
ASER17
ATHR35
AGCP201
AHOH301
AHOH302

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 203
ChainResidue
AGLY10
AALA59
AGLY60
ATYR96
AHOH305
AHOH365

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 204
ChainResidue
ALYS101
AASP105
ASER106
AGLU107

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 205
ChainResidue
ATHR35
AILE36
AGLU37
AASP38
ATHR148

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

PDB statisticsPDBj update infoContact PDBjnumon