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

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
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
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 Residues8
DetailsMotif: {"description":"Effector region","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P61586","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P62820","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosylasparagine; by botulinum toxin","evidences":[{"source":"UniProtKB","id":"P61586","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsGlycosylation: {"description":"(Microbial infection) O-linked (Glc) threonine; by C.difficile toxin TcdB; alternate","evidences":[{"source":"PubMed","id":"24905543","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"17947660","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18034455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

PDB statisticsPDBj update infoContact PDBjnumon