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4A9A

Structure of Rbg1 in complex with Tma46 dfrp domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002181biological_processcytoplasmic translation
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005777cellular_componentperoxisome
A0010494cellular_componentcytoplasmic stress granule
A1903833biological_processpositive regulation of cellular response to amino acid starvation
B0000166molecular_functionnucleotide binding
B0002181biological_processcytoplasmic translation
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005777cellular_componentperoxisome
B0010494cellular_componentcytoplasmic stress granule
B1903833biological_processpositive regulation of cellular response to amino acid starvation
Functional Information from PROSITE/UniProt
site_idPS00905
Number of Residues14
DetailsGTP1_OBG GTP1/OBG family signature. DLPGIIDGAkdGrG
ChainResidueDetails
AASP118-GLY131

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues152
DetailsDomain: {"description":"TGS","evidences":[{"source":"PROSITE-ProRule","id":"PRU01228","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01047","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues11
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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