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6UKA

Crystal structure of RHOG and ELMO complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0007015biological_processactin filament organization
A0007163biological_processestablishment or maintenance of cell polarity
A0007264biological_processsmall GTPase-mediated signal transduction
A0007266biological_processRho protein signal transduction
A0008284biological_processpositive regulation of cell population proliferation
A0008360biological_processregulation of cell shape
A0016020cellular_componentmembrane
A0016601biological_processRac protein signal transduction
A0019901molecular_functionprotein kinase binding
A0030036biological_processactin cytoskeleton organization
A0030667cellular_componentsecretory granule membrane
A0030865biological_processcortical cytoskeleton organization
A0031410cellular_componentcytoplasmic vesicle
A0032956biological_processregulation of actin cytoskeleton organization
A0042995cellular_componentcell projection
A0045893biological_processpositive regulation of DNA-templated transcription
A0060326biological_processcell chemotaxis
A0070062cellular_componentextracellular exosome
A0090630biological_processactivation of GTPase activity
A0098794cellular_componentpostsynapse
A0098978cellular_componentglutamatergic synapse
A0150052biological_processregulation of postsynapse assembly
A1900027biological_processregulation of ruffle assembly
A1903078biological_processpositive regulation of protein localization to plasma membrane
Functional Information from PDB Data
site_idAC1
Number of Residues25
Detailsbinding site for residue GNP A 201
ChainResidue
AGLY12
APRO34
ATHR35
AGLY60
ALYS116
AASP118
ALEU119
ASER158
AALA159
ALEU160
AMG202
AALA13
AHOH314
AHOH317
AHOH321
AHOH329
AHOH349
AHOH352
AVAL14
AGLY15
ALYS16
ATHR17
ACYS18
APHE28
ATYR32

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 202
ChainResidue
ATHR17
ATHR35
AGNP201
AHOH314
AHOH317

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:17947660, ECO:0007744|PubMed:18034455
ChainResidueDetails
BTYR48
ATHR115

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P62820
ChainResidueDetails
APHE28
AASP57

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: ADP-ribosylasparagine; by botulinum toxin => ECO:0000250|UniProtKB:P61586
ChainResidueDetails
AASN39

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR138
ATHR180

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Cysteine methyl ester => ECO:0000250|UniProtKB:P61586
ChainResidueDetails
ACYS188

site_idSWS_FT_FI6
Number of Residues1
DetailsLIPID: S-geranylgeranyl cysteine => ECO:0000250|UniProtKB:P61586
ChainResidueDetails
ACYS188

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: (Microbial infection) O-linked (Glc) threonine; by C.difficile toxin TcdB; alternate => ECO:0000269|PubMed:24905543
ChainResidueDetails
ATHR35

236371

PDB entries from 2025-05-21

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