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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6O22

Structure of Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000785cellular_componentchromatin
A0003682molecular_functionchromatin binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0006303biological_processdouble-strand break repair via nonhomologous end joining
A0006325biological_processchromatin organization
A0006334biological_processnucleosome assembly
A0006335biological_processDNA replication-dependent chromatin assembly
A0010698molecular_functionacetyltransferase activator activity
A0015031biological_processprotein transport
A0042393molecular_functionhistone binding
A0042802molecular_functionidentical protein binding
A0070775cellular_componentH3 histone acetyltransferase complex
A2000617biological_processobsolete positive regulation of histone H3-K9 acetylation
B0000785cellular_componentchromatin
B0003682molecular_functionchromatin binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005829cellular_componentcytosol
B0006303biological_processdouble-strand break repair via nonhomologous end joining
B0006325biological_processchromatin organization
B0006334biological_processnucleosome assembly
B0006335biological_processDNA replication-dependent chromatin assembly
B0010698molecular_functionacetyltransferase activator activity
B0015031biological_processprotein transport
B0042393molecular_functionhistone binding
B0042802molecular_functionidentical protein binding
B0070775cellular_componentH3 histone acetyltransferase complex
B2000617biological_processobsolete positive regulation of histone H3-K9 acetylation
C0000785cellular_componentchromatin
C0004402molecular_functionhistone acetyltransferase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0006325biological_processchromatin organization
C0006335biological_processDNA replication-dependent chromatin assembly
C0006338biological_processchromatin remodeling
C0006351biological_processDNA-templated transcription
C0006357biological_processregulation of transcription by RNA polymerase II
C0006974biological_processDNA damage response
C0010468biological_processregulation of gene expression
C0010484molecular_functionhistone H3 acetyltransferase activity
C0010526biological_processtransposable element silencing
C0016740molecular_functiontransferase activity
C0032931molecular_functionhistone H3K56 acetyltransferase activity
C0033554biological_processcellular response to stress
C0036408molecular_functionhistone H3K14 acetyltransferase activity
C0043007biological_processmaintenance of rDNA
C0043992molecular_functionhistone H3K9 acetyltransferase activity
C0043994molecular_functionhistone H3K23 acetyltransferase activity
C0044017molecular_functionhistone H3K27 acetyltransferase activity
C0061733molecular_functionprotein-lysine-acetyltransferase activity
C0070775cellular_componentH3 histone acetyltransferase complex
C1990414biological_processreplication-born double-strand break repair via sister chromatid exchange
C2001032biological_processregulation of double-strand break repair via nonhomologous end joining
D0000781cellular_componentchromosome, telomeric region
D0000785cellular_componentchromatin
D0001932biological_processregulation of protein phosphorylation
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005829cellular_componentcytosol
D0006282biological_processregulation of DNA repair
D0006325biological_processchromatin organization
D0006335biological_processDNA replication-dependent chromatin assembly
D0006337biological_processnucleosome disassembly
D0006338biological_processchromatin remodeling
D0006351biological_processDNA-templated transcription
D0006357biological_processregulation of transcription by RNA polymerase II
D0010468biological_processregulation of gene expression
D0010698molecular_functionacetyltransferase activator activity
D0030466biological_processsilent mating-type cassette heterochromatin formation
D0031509biological_processsubtelomeric heterochromatin formation
D0032968biological_processpositive regulation of transcription elongation by RNA polymerase II
D0033554biological_processcellular response to stress
D0042393molecular_functionhistone binding
D0070775cellular_componentH3 histone acetyltransferase complex
D2000002biological_processnegative regulation of DNA damage checkpoint
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0030527molecular_functionstructural constituent of chromatin
E0031492molecular_functionnucleosomal DNA binding
E0031507biological_processheterochromatin formation
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005694cellular_componentchromosome
F0006334biological_processnucleosome assembly
F0030527molecular_functionstructural constituent of chromatin
F0031507biological_processheterochromatin formation
Functional Information from PROSITE/UniProt
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
FGLY14-HIS18
site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
ELYS14-LEU20
site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
EPRO66-ILE74
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues402
DetailsDomain: {"description":"Rtt109-type HAT","evidences":[{"source":"PROSITE-ProRule","id":"PRU01064","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues42
DetailsRegion: {"description":"Interaction with VPS75","evidences":[{"source":"PubMed","id":"18719104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21256037","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21454705","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"18707894","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18568037","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18707894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18719104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21256037","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZFN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CZ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3Q33","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3Q35","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QM0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18568037","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QM0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18568037","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21256037","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3Q33","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3Q35","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QM0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18707894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18719104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21256037","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZFN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CZ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3Q33","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3Q35","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"18568037","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18707894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18719104","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84228","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsModified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
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_FI25
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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