2ZFN
Self-acetylation mediated histone H3 lysine 56 acetylation by rtt109
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000785 | cellular_component | chromatin |
A | 0004402 | molecular_function | histone acetyltransferase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0006325 | biological_process | chromatin organization |
A | 0006334 | biological_process | nucleosome assembly |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
A | 0006974 | biological_process | DNA damage response |
A | 0010468 | biological_process | regulation of gene expression |
A | 0010484 | molecular_function | histone H3 acetyltransferase activity |
A | 0010526 | biological_process | retrotransposon silencing |
A | 0016740 | molecular_function | transferase activity |
A | 0032931 | molecular_function | histone H3K56 acetyltransferase activity |
A | 0033554 | biological_process | cellular response to stress |
A | 0036211 | biological_process | protein modification process |
A | 0036408 | molecular_function | histone H3K14 acetyltransferase activity |
A | 0043007 | biological_process | maintenance of rDNA |
A | 0043992 | molecular_function | histone H3K9 acetyltransferase activity |
A | 0043994 | molecular_function | histone H3K23 acetyltransferase activity |
A | 0044017 | molecular_function | histone H3K27 acetyltransferase activity |
A | 0061733 | molecular_function | peptide-lysine-N-acetyltransferase activity |
A | 0070775 | cellular_component | H3 histone acetyltransferase complex |
A | 1990414 | biological_process | replication-born double-strand break repair via sister chromatid exchange |
A | 2001032 | biological_process | regulation of double-strand break repair via nonhomologous end joining |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE ACO A 500 |
Chain | Residue |
A | SER86 |
A | ALA196 |
A | TYR199 |
A | LYS210 |
A | HIS211 |
A | ILE212 |
A | LEU213 |
A | LEU218 |
A | TRP221 |
A | TRP222 |
A | THR271 |
A | LYS87 |
A | SER272 |
A | HOH803 |
A | HOH851 |
A | HOH867 |
A | HOH901 |
A | ALA88 |
A | ASP89 |
A | THR90 |
A | ARG101 |
A | PHE192 |
A | ARG194 |
A | PRO195 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 601 |
Chain | Residue |
A | SER86 |
A | LYS87 |
A | PHE192 |
A | TYR199 |
A | ASP287 |
A | PRO289 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:18707894 |
Chain | Residue | Details |
A | ASP288 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | ALA88 | |
A | ARG97 | |
A | HIS211 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18568037, ECO:0007744|PDB:3QM0 |
Chain | Residue | Details |
A | PHE192 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18568037, ECO:0000269|PubMed:21256037, ECO:0007744|PDB:3Q33, ECO:0007744|PDB:3Q35, ECO:0007744|PDB:3QM0 |
Chain | Residue | Details |
A | ALA196 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | TRP221 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:18568037, ECO:0000269|PubMed:18707894, ECO:0000269|PubMed:18719104 |
Chain | Residue | Details |
A | ALY290 |