1XQH
Crystal structure of a ternary complex of the methyltransferase SET9 (also known as SET7/9) with a P53 peptide and SAH
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 |
| E | 0005694 | cellular_component | chromosome |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| E | 0140945 | molecular_function | histone H3K4 monomethyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE SAH A 1501 |
| Chain | Residue |
| A | ALA226 |
| A | GLU356 |
| A | HOH1522 |
| A | HOH1526 |
| A | HOH1530 |
| A | HOH1535 |
| A | HOH1536 |
| A | HOH1621 |
| A | HOH1702 |
| A | HOH1709 |
| B | MLZ372 |
| A | GLU228 |
| A | ASN265 |
| A | HIS293 |
| A | LYS294 |
| A | ASN296 |
| A | HIS297 |
| A | TYR335 |
| A | TRP352 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE SAH E 2501 |
| Chain | Residue |
| E | ALA226 |
| E | GLY227 |
| E | GLU228 |
| E | ASN265 |
| E | HIS293 |
| E | LYS294 |
| E | ASN296 |
| E | HIS297 |
| E | TYR335 |
| E | TRP352 |
| E | GLU356 |
| E | HOH2523 |
| E | HOH2528 |
| E | HOH2532 |
| E | HOH2535 |
| E | HOH2540 |
| E | HOH2667 |
| E | HOH2687 |
| E | HOH2708 |
| E | HOH2757 |
| F | MLZ372 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 244 |
| Details | Domain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| 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_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12514135","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12540855","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| 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 | Annotated By Reference To The Literature 1h3i |
| Chain | Residue | Details |
| A | TYR335 | |
| A | HIS293 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1h3i |
| Chain | Residue | Details |
| E | TYR335 | |
| E | 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 |
