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2RIM

Crystal structure of Rtt109

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
A0043994molecular_functionhistone H3K23 acetyltransferase activity
A0044017molecular_functionhistone H3K27 acetyltransferase activity
A0061733molecular_functionpeptide-lysine-N-acetyltransferase activity
A0070775cellular_componentH3 histone acetyltransferase complex
A1990414biological_processreplication-born double-strand break repair via sister chromatid exchange
A2001032biological_processregulation of double-strand break repair via nonhomologous end joining
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:18707894
ChainResidueDetails
AASP288

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:18568037, 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, ECO:0007744|PDB:3QM0
ChainResidueDetails
AALA88
AARG97
AHIS211

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18568037, ECO:0007744|PDB:3QM0
ChainResidueDetails
APHE192

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
ALYS290

223790

PDB entries from 2024-08-14

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