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 | 44 |
| Details | Repeat: {"description":"MORN 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 44 |
| Details | Repeat: {"description":"MORN 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 244 |
| Details | Domain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12514135","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12540855","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | Site: {"description":"Histone H3K4 binding","evidences":[{"source":"PubMed","id":"12540855","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 12514135 |
| Chain | Residue | Details |
| A | TYR335 | |
| A | HIS293 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 12514135 |
| Chain | Residue | Details |
| B | TYR335 | |
| B | HIS293 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 350 |
| Chain | Residue | Details |
| A | TYR245 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | HIS293 | electrostatic stabiliser, hydrogen bond acceptor |
| A | HIS297 | electrostatic stabiliser, hydrogen bond acceptor |
| A | TYR305 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | TYR335 | 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 | TYR245 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | HIS293 | electrostatic stabiliser, hydrogen bond acceptor |
| B | HIS297 | electrostatic stabiliser, hydrogen bond acceptor |
| B | TYR305 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| B | TYR335 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
