Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005634 | cellular_component | nucleus |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0004402 | molecular_function | histone acetyltransferase activity |
| B | 0006338 | biological_process | chromatin remodeling |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 301 |
| Chain | Residue |
| B | HIS125 |
| B | CYS129 |
| B | CYS142 |
| B | CYS147 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 302 |
| Chain | Residue |
| B | HIS156 |
| B | CYS160 |
| B | CYS166 |
| B | CYS171 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 303 |
| Chain | Residue |
| B | CYS184 |
| B | CYS189 |
| B | VAL191 |
| B | CYS192 |
| B | HIS180 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 86 |
| Details | Zinc finger: {"description":"TAZ-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00203","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11959990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12778114","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18995842","evidenceCode":"ECO:0000269"}]} |
1P4Q
