1H3I
Crystal structure of the Histone Methyltransferase SET7/9
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005694 | cellular_component | chromosome |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| A | 0140945 | molecular_function | histone H3K4 monomethyltransferase activity |
| B | 0005694 | cellular_component | chromosome |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| B | 0140945 | molecular_function | histone H3K4 monomethyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A1345 |
| Chain | Residue |
| A | HOH2133 |
| A | HOH2134 |
| A | HOH2147 |
| A | HOH2149 |
| A | HOH2150 |
| B | HOH2119 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A1346 |
| Chain | Residue |
| B | HIS283 |
| A | GLU279 |
| A | HIS283 |
| B | GLU279 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B1346 |
| Chain | Residue |
| A | HOH2128 |
| B | HOH2123 |
| B | HOH2125 |
| B | HOH2140 |
| B | HOH2141 |
| B | HOH2143 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12514135, ECO:0000269|PubMed:12540855 |
| Chain | Residue | Details |
| A | LEU172 | |
| A | MET242 | |
| A | SER243 | |
| B | LEU172 | |
| B | MET242 | |
| B | SER243 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00190, ECO:0000269|PubMed:12514135, ECO:0000269|PubMed:12540855 |
| Chain | Residue | Details |
| A | ASN302 | |
| B | ASN302 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | SITE: Histone H3K4 binding => ECO:0000269|PubMed:12540855 |
| Chain | Residue | Details |
| A | TYR191 | |
| B | TYR281 | |
| A | SER202 | |
| A | GLU212 | |
| A | ASN263 | |
| A | TYR281 | |
| B | TYR191 | |
| B | SER202 | |
| B | GLU212 | |
| B | ASN263 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 350 |
| Chain | Residue | Details |
| A | TYR191 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | ASN239 | electrostatic stabiliser, hydrogen bond acceptor |
| A | SER243 | electrostatic stabiliser, hydrogen bond acceptor |
| A | THR251 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | TYR281 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 350 |
| Chain | Residue | Details |
| B | TYR191 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | ASN239 | electrostatic stabiliser, hydrogen bond acceptor |
| B | SER243 | electrostatic stabiliser, hydrogen bond acceptor |
| B | THR251 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| B | TYR281 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
