7C3O
Crystal structure of TT109 from CANDIDA ALBICANS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004402 | molecular_function | histone acetyltransferase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0006325 | biological_process | chromatin organization |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0006351 | biological_process | DNA-templated transcription |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0006974 | biological_process | DNA damage response |
| A | 0010484 | molecular_function | histone H3 acetyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030447 | biological_process | filamentous growth |
| A | 0032931 | molecular_function | histone H3K56 acetyltransferase activity |
| A | 0036166 | biological_process | phenotypic switching |
| A | 0044182 | biological_process | filamentous growth of a population of unicellular organisms |
| A | 0061733 | molecular_function | protein-lysine-acetyltransferase activity |
| A | 1900239 | biological_process | regulation of phenotypic switching |
| A | 1900429 | biological_process | negative regulation of filamentous growth of a population of unicellular organisms |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | binding site for residue ACO A 401 |
| Chain | Residue |
| A | CYS81 |
| A | TYR183 |
| A | LYS194 |
| A | ASN195 |
| A | LEU196 |
| A | LEU197 |
| A | LEU202 |
| A | TRP205 |
| A | TRP206 |
| A | HOH502 |
| A | HOH545 |
| A | ASP82 |
| A | HOH575 |
| A | HOH595 |
| A | HOH612 |
| A | HOH619 |
| A | THR83 |
| A | LYS92 |
| A | ILE93 |
| A | GLY94 |
| A | PHE176 |
| A | LYS178 |
| A | ALA180 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | THR22 |
| A | ILE24 |
| A | LYS42 |
| A | ARG44 |
| A | ILE327 |
| A | HOH519 |
| A | HOH544 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 403 |
| Chain | Residue |
| A | THR326 |
| A | GLU329 |
| A | HOH528 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue PEG A 404 |
| Chain | Residue |
| A | LYS281 |
| A | MET282 |
| A | THR283 |
| A | SER285 |
| A | ARG286 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"Q07794","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q07794","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q07794","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
