3Q33
Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation
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 | 0006335 | biological_process | DNA replication-dependent chromatin assembly |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0006351 | biological_process | DNA-templated transcription |
| 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 | transposable element silencing |
| A | 0016740 | molecular_function | transferase activity |
| A | 0032931 | molecular_function | histone H3K56 acetyltransferase activity |
| A | 0033554 | biological_process | cellular response to stress |
| 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 | protein-lysine-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 |
| B | 0005634 | cellular_component | nucleus |
| B | 0006334 | biological_process | nucleosome assembly |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NH2 D 15 |
| Chain | Residue |
| A | GLY367 |
| D | GLY13 |
| D | LYS14 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ACO A 501 |
| Chain | Residue |
| A | VAL100 |
| A | ARG101 |
| A | PHE192 |
| A | PRO195 |
| A | ALA196 |
| A | TYR199 |
| A | LYS210 |
| A | HIS211 |
| A | LEU213 |
| A | LEU218 |
| A | TRP221 |
| A | TRP222 |
| A | EDO502 |
| A | VAL85 |
| A | SER86 |
| A | ALA88 |
| A | ASP89 |
| A | THR90 |
| A | VAL98 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 502 |
| Chain | Residue |
| A | SER86 |
| A | PHE192 |
| A | ARG194 |
| A | TYR199 |
| A | ACO501 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR CHAIN D OF HISTONE H3 |
| Chain | Residue |
| A | LYS363 |
| A | GLY367 |
| A | GLU368 |
| A | GLU369 |
| B | ASN70 |
| B | ILE72 |
| B | HIS196 |
| B | SER199 |
| D | NH215 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"18707894","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18568037","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QM0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-butyryllysine; alternate","evidences":[{"source":"PubMed","id":"19113941","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27105113","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
