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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9DTQ

The structure of HDAC2-CoREST in complex with KBTBD4R313PRR mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0000118cellular_componenthistone deacetylase complex
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000781cellular_componentchromosome, telomeric region
A0000785cellular_componentchromatin
A0001221molecular_functiontranscription coregulator binding
A0003682molecular_functionchromatin binding
A0003723molecular_functionRNA binding
A0004407molecular_functionhistone deacetylase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0006338biological_processchromatin remodeling
A0008284biological_processpositive regulation of cell population proliferation
A0009913biological_processepidermal cell differentiation
A0010977biological_processnegative regulation of neuron projection development
A0016358biological_processdendrite development
A0016581cellular_componentNuRD complex
A0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A0017053cellular_componenttranscription repressor complex
A0019899molecular_functionenzyme binding
A0030336biological_processnegative regulation of cell migration
A0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
A0031492molecular_functionnucleosomal DNA binding
A0031507biological_processheterochromatin formation
A0032922biological_processcircadian regulation of gene expression
A0032991cellular_componentprotein-containing complex
A0033148biological_processpositive regulation of intracellular estrogen receptor signaling pathway
A0033558molecular_functionprotein lysine deacetylase activity
A0035098cellular_componentESC/E(Z) complex
A0042393molecular_functionhistone binding
A0042475biological_processodontogenesis of dentin-containing tooth
A0042659biological_processregulation of cell fate specification
A0042733biological_processembryonic digit morphogenesis
A0042826molecular_functionhistone deacetylase binding
A0043066biological_processnegative regulation of apoptotic process
A0045862biological_processpositive regulation of proteolysis
A0045892biological_processnegative regulation of DNA-templated transcription
A0045893biological_processpositive regulation of DNA-templated transcription
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0045995biological_processregulation of embryonic development
A0050847biological_processprogesterone receptor signaling pathway
A0051059molecular_functionNF-kappaB binding
A0060789biological_processhair follicle placode formation
A0061029biological_processeyelid development in camera-type eye
A0061198biological_processfungiform papilla formation
A0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
A0070822cellular_componentSin3-type complex
A0141221molecular_functionhistone deacetylase activity, hydrolytic mechanism
A0160008molecular_functionprotein decrotonylase activity
A0160009molecular_functionhistone decrotonylase activity
A0160010molecular_functionprotein de-2-hydroxyisobutyrylase activity
A0160216molecular_functionprotein lysine delactylase activity
A1902455biological_processnegative regulation of stem cell population maintenance
A1902459biological_processpositive regulation of stem cell population maintenance
A2000736biological_processregulation of stem cell differentiation
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues313
DetailsRegion: {"description":"Histone deacetylase"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"Q13547","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O15379","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37137925","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8BPA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8BPB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8BPC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37137925","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8BPB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8BPC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q13547","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q13547","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P70288","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues134
DetailsDomain: {"description":"BTB","evidences":[{"source":"PROSITE-ProRule","id":"PRU00037","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues184
DetailsDomain: {"description":"BACK"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues92
DetailsRepeat: {"description":"Kelch 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues94
DetailsRepeat: {"description":"Kelch 3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues100
DetailsRepeat: {"description":"Kelch 4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues98
DetailsRepeat: {"description":"Kelch 5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

254917

PDB entries from 2026-06-10

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