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9V2V

Cryo-EM structure of the histone deacetylase complex Rpd3L in complex with mono-nucleosome

Functional Information from GO Data
ChainGOidnamespacecontents
F0000122biological_processnegative regulation of transcription by RNA polymerase II
F0004407molecular_functionhistone deacetylase activity
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005829cellular_componentcytosol
F0006334biological_processnucleosome assembly
F0006357biological_processregulation of transcription by RNA polymerase II
F0031507biological_processheterochromatin formation
F0033698cellular_componentRpd3L complex
F0034605biological_processcellular response to heat
F0042826molecular_functionhistone deacetylase binding
F0043709biological_processcell adhesion involved in single-species biofilm formation
F0045944biological_processpositive regulation of transcription by RNA polymerase II
F0061186biological_processnegative regulation of silent mating-type cassette heterochromatin formation
F0061188biological_processnegative regulation of rDNA heterochromatin formation
F0070210cellular_componentRpd3L-Expanded complex
F0070822cellular_componentSin3-type complex
F2000217biological_processregulation of invasive growth in response to glucose limitation
Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
OALA21-VAL27

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
PARG89-GLY111

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
QPRO66-ILE74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues624
DetailsRegion: {"description":"Histone deacetylase"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsMotif: {"description":"ESA1-RPD3 motif"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues74
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"N6-methacryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

255900

PDB entries from 2026-07-01

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