5J9Q
Crystal structure of the NuA4 core complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004402 | molecular_function | histone acetyltransferase activity |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0000123 | cellular_component | histone acetyltransferase complex |
| B | 0004402 | molecular_function | histone acetyltransferase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0006281 | biological_process | DNA repair |
| B | 0006338 | biological_process | chromatin remodeling |
| B | 0006351 | biological_process | DNA-templated transcription |
| B | 0033100 | cellular_component | NuA3 histone acetyltransferase complex |
| B | 0035267 | cellular_component | NuA4 histone acetyltransferase complex |
| B | 1990467 | cellular_component | NuA3a histone acetyltransferase complex |
| B | 1990468 | cellular_component | NuA3b histone acetyltransferase complex |
| C | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| C | 0035267 | cellular_component | NuA4 histone acetyltransferase complex |
| E | 0004402 | molecular_function | histone acetyltransferase activity |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
| F | 0000123 | cellular_component | histone acetyltransferase complex |
| F | 0004402 | molecular_function | histone acetyltransferase activity |
| F | 0005634 | cellular_component | nucleus |
| F | 0006281 | biological_process | DNA repair |
| F | 0006338 | biological_process | chromatin remodeling |
| F | 0006351 | biological_process | DNA-templated transcription |
| F | 0033100 | cellular_component | NuA3 histone acetyltransferase complex |
| F | 0035267 | cellular_component | NuA4 histone acetyltransferase complex |
| F | 1990467 | cellular_component | NuA3a histone acetyltransferase complex |
| F | 1990468 | cellular_component | NuA3b histone acetyltransferase complex |
| G | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| G | 0035267 | cellular_component | NuA4 histone acetyltransferase complex |
| I | 0004402 | molecular_function | histone acetyltransferase activity |
| I | 0006355 | biological_process | regulation of DNA-templated transcription |
| J | 0000123 | cellular_component | histone acetyltransferase complex |
| J | 0004402 | molecular_function | histone acetyltransferase activity |
| J | 0005634 | cellular_component | nucleus |
| J | 0006281 | biological_process | DNA repair |
| J | 0006338 | biological_process | chromatin remodeling |
| J | 0006351 | biological_process | DNA-templated transcription |
| J | 0033100 | cellular_component | NuA3 histone acetyltransferase complex |
| J | 0035267 | cellular_component | NuA4 histone acetyltransferase complex |
| J | 1990467 | cellular_component | NuA3a histone acetyltransferase complex |
| J | 1990468 | cellular_component | NuA3b histone acetyltransferase complex |
| N | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| N | 0035267 | cellular_component | NuA4 histone acetyltransferase complex |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 75 |
| Details | Zinc finger: {"description":"C2HC MYST-type; degenerate","evidences":[{"source":"PROSITE-ProRule","id":"PRU01063","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"12368900","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"17223684","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"18245364","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000303"},{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 33 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11106757","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12368900","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 279 |
| Details | Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"16543222","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16543223","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 525 |
| Chain | Residue | Details |
| A | LEU308 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | SER342 | activator, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 525 |
| Chain | Residue | Details |
| site_id | MCSA3 |
| Number of Residues | 2 |
| Details | M-CSA 525 |
| Chain | Residue | Details |
| E | LEU308 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| E | SER342 | activator, proton acceptor, proton donor |
