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7X3K

Cryo-EM structure of RAC in the State C2 RNC-RAC complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000054biological_processribosomal subunit export from nucleus
A0003677molecular_functionDNA binding
A0003713molecular_functiontranscription coactivator activity
A0005515molecular_functionprotein binding
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005840cellular_componentribosome
A0006364biological_processrRNA processing
A0006450biological_processregulation of translational fidelity
A0006452biological_processtranslational frameshifting
A0006457biological_processprotein folding
A0015934cellular_componentlarge ribosomal subunit
A0015935cellular_componentsmall ribosomal subunit
A0030544molecular_functionHsp70 protein binding
A0035556biological_processintracellular signal transduction
A0042788cellular_componentobsolete polysomal ribosome
A0043022molecular_functionribosome binding
A0045893biological_processpositive regulation of DNA-templated transcription
A0051083biological_process'de novo' cotranslational protein folding
A0101031cellular_componentprotein folding chaperone complex
B0002181biological_processcytoplasmic translation
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006364biological_processrRNA processing
B0006450biological_processregulation of translational fidelity
B0006452biological_processtranslational frameshifting
B0006457biological_processprotein folding
B0016887molecular_functionATP hydrolysis activity
B0031072molecular_functionheat shock protein binding
B0042026biological_processprotein refolding
B0044183molecular_functionprotein folding chaperone
B0051082molecular_functionunfolded protein binding
B0051083biological_process'de novo' cotranslational protein folding
B0051085biological_processchaperone cofactor-dependent protein refolding
B0101031cellular_componentprotein folding chaperone complex
B0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PROSITE/UniProt
site_idPS00636
Number of Residues20
DetailsDNAJ_1 Nt-dnaJ domain signature. FKiIQkaFEtLtDsnkRAQY
ChainResidueDetails
APHE145-TYR164

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
BSER477

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
BSER480

221716

PDB entries from 2024-06-26

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