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 | 0006289 | biological_process | nucleotide-excision repair |
A | 0006325 | biological_process | chromatin organization |
A | 0006338 | biological_process | chromatin remodeling |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0006890 | biological_process | retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum |
A | 0006896 | biological_process | Golgi to vacuole transport |
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 | 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 | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q07794 |
Chain | Residue | Details |
A | ASP264 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q07794 |
Chain | Residue | Details |
A | PHE176 | |
A | ALA180 | |
A | ASN195 | |
A | TRP205 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000250|UniProtKB:Q07794 |
Chain | Residue | Details |
A | ALY266 |