1U2Z
Crystal structure of histone K79 methyltransferase Dot1p from yeast
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000077 | biological_process | DNA damage checkpoint signaling |
| A | 0000786 | cellular_component | nucleosome |
| A | 0006281 | biological_process | DNA repair |
| A | 0031151 | molecular_function | histone H3K79 methyltransferase activity |
| A | 0031509 | biological_process | subtelomeric heterochromatin formation |
| A | 0042393 | molecular_function | histone binding |
| A | 0051726 | biological_process | regulation of cell cycle |
| B | 0000077 | biological_process | DNA damage checkpoint signaling |
| B | 0000786 | cellular_component | nucleosome |
| B | 0006281 | biological_process | DNA repair |
| B | 0031151 | molecular_function | histone H3K79 methyltransferase activity |
| B | 0031509 | biological_process | subtelomeric heterochromatin formation |
| B | 0042393 | molecular_function | histone binding |
| B | 0051726 | biological_process | regulation of cell cycle |
| C | 0000077 | biological_process | DNA damage checkpoint signaling |
| C | 0000786 | cellular_component | nucleosome |
| C | 0006281 | biological_process | DNA repair |
| C | 0031151 | molecular_function | histone H3K79 methyltransferase activity |
| C | 0031509 | biological_process | subtelomeric heterochromatin formation |
| C | 0042393 | molecular_function | histone binding |
| C | 0051726 | biological_process | regulation of cell cycle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE SAH A 801 |
| Chain | Residue |
| A | ASN369 |
| A | MET424 |
| A | SER459 |
| A | PHE460 |
| A | ASN479 |
| A | HOH802 |
| A | HOH814 |
| A | HOH867 |
| A | HOH874 |
| A | HOH916 |
| C | GLU197 |
| A | TYR370 |
| A | GLY373 |
| A | LEU375 |
| A | ASP397 |
| A | GLY399 |
| A | CYS405 |
| A | GLU422 |
| A | ILE423 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE SAH B 802 |
| Chain | Residue |
| B | ASN369 |
| B | TYR370 |
| B | GLY373 |
| B | LEU375 |
| B | ASP397 |
| B | GLY399 |
| B | CYS405 |
| B | GLU422 |
| B | ILE423 |
| B | MET424 |
| B | SER459 |
| B | PHE460 |
| B | ASN479 |
| B | HOH805 |
| B | HOH806 |
| B | HOH810 |
| B | HOH811 |
| B | HOH812 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE SAH C 803 |
| Chain | Residue |
| C | ASN369 |
| C | TYR370 |
| C | GLY373 |
| C | LEU375 |
| C | ASP397 |
| C | GLY399 |
| C | CYS405 |
| C | GLU422 |
| C | ILE423 |
| C | MET424 |
| C | SER459 |
| C | PHE460 |
| C | ASN479 |
| C | LEU487 |
| C | HOH805 |
| C | HOH825 |
| C | HOH830 |
| C | HOH858 |
| C | HOH878 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | TYR372 | |
| C | PHE395 | |
| C | GLU422 | |
| C | SER459 | |
| A | PHE395 | |
| A | GLU422 | |
| A | SER459 | |
| B | TYR372 | |
| B | PHE395 | |
| B | GLU422 | |
| B | SER459 | |
| C | TYR372 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine; by HOG1 => ECO:0000269|PubMed:38270553 |
| Chain | Residue | Details |
| A | SER565 | |
| B | SER565 | |
| C | SER565 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphothreonine; by HOG1 => ECO:0000269|PubMed:38270553 |
| Chain | Residue | Details |
| A | THR576 | |
| B | THR576 | |
| C | THR576 |
