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3Q33

Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000785cellular_componentchromatin
A0004402molecular_functionhistone acetyltransferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0006325biological_processchromatin organization
A0006334biological_processnucleosome assembly
A0006355biological_processregulation of DNA-templated transcription
A0006357biological_processregulation of transcription by RNA polymerase II
A0006974biological_processDNA damage response
A0010468biological_processregulation of gene expression
A0010484molecular_functionhistone H3 acetyltransferase activity
A0010526biological_processretrotransposon silencing
A0016740molecular_functiontransferase activity
A0032931molecular_functionhistone H3K56 acetyltransferase activity
A0033554biological_processcellular response to stress
A0036211biological_processprotein modification process
A0036408molecular_functionhistone H3K14 acetyltransferase activity
A0043007biological_processmaintenance of rDNA
A0043992molecular_functionhistone H3K9 acetyltransferase activity
A0043993molecular_functionhistone H3K18 acetyltransferase activity
A0043994molecular_functionhistone H3K23 acetyltransferase activity
A0043995molecular_functionhistone H4K5 acetyltransferase activity
A0043996molecular_functionhistone H4K8 acetyltransferase activity
A0043997molecular_functionhistone H4K12 acetyltransferase activity
A0043999molecular_functionhistone H2AK5 acetyltransferase activity
A0044012molecular_functionhistone H2AK9 acetyltransferase activity
A0044014molecular_functionhistone H2BK5 acetyltransferase activity
A0044015molecular_functionhistone H2BK12 acetyltransferase activity
A0044016molecular_functionhistone H3K4 acetyltransferase activity
A0044017molecular_functionhistone H3K27 acetyltransferase activity
A0044018molecular_functionhistone H3K36 acetyltransferase activity
A0046972molecular_functionhistone H4K16 acetyltransferase activity
A0061733molecular_functionpeptide-lysine-N-acetyltransferase activity
A0070775cellular_componentH3 histone acetyltransferase complex
A0140908molecular_functionhistone H3K122 acetyltransferase activity
A1990414biological_processreplication-born double-strand break repair via sister chromatid exchange
A2001032biological_processregulation of double-strand break repair via nonhomologous end joining
B0005634cellular_componentnucleus
B0006334biological_processnucleosome assembly
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NH2 D 15
ChainResidue
AGLY367
DGLY13
DLYS14

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ACO A 501
ChainResidue
AVAL100
AARG101
APHE192
APRO195
AALA196
ATYR199
ALYS210
AHIS211
ALEU213
ALEU218
ATRP221
ATRP222
AEDO502
AVAL85
ASER86
AALA88
AASP89
ATHR90
AVAL98

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 502
ChainResidue
ASER86
APHE192
AARG194
ATYR199
AACO501

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR CHAIN D OF HISTONE H3
ChainResidue
ALYS363
AGLY367
AGLU368
AGLU369
BASN70
BILE72
BHIS196
BSER199
DNH215

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:11742990, ECO:0000269|PubMed:11751634, ECO:0000269|PubMed:11752412, ECO:0000269|PubMed:12152067, ECO:0000269|PubMed:12353038, ECO:0000269|PubMed:12845608, ECO:0000269|PubMed:15949446, ECO:0000269|PubMed:16122352, ECO:0000269|PubMed:16168379, ECO:0000269|PubMed:16185711, ECO:0000269|PubMed:17194708
ChainResidueDetails
DGLN5

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:17194708
ChainResidueDetails
DSER10
AARG97
AHIS211

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:10911986, ECO:0000269|PubMed:10975519, ECO:0000269|PubMed:15719021
ChainResidueDetails
DTHR11

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18568037, ECO:0000269|PubMed:21256037, ECO:0007744|PDB:3Q33, ECO:0007744|PDB:3Q35, ECO:0007744|PDB:3QM0
ChainResidueDetails
AALA196

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18707894, ECO:0000269|PubMed:18719104, ECO:0000269|PubMed:21256037, ECO:0007744|PDB:2ZFN, ECO:0007744|PDB:3CZ7, ECO:0007744|PDB:3Q33, ECO:0007744|PDB:3Q35
ChainResidueDetails
ATRP221

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:18568037, ECO:0000269|PubMed:18707894, ECO:0000269|PubMed:18719104
ChainResidueDetails
AALY290

227344

PDB entries from 2024-11-13

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