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 | 2 |
Details | MOD_RES: N6-methyllysine; by SMYD2; alternate => ECO:0000269|PubMed:17108971, ECO:0000269|PubMed:22864287 |
Chain | Residue | Details |
B | LYS370 | |
F | LYS370 | |
A | HIS297 | |
E | ALA226 | |
E | ASN296 | |
E | HIS297 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; by SETD7 => ECO:0000269|PubMed:15525938, ECO:0000269|PubMed:16415881 |
Chain | Residue | Details |
B | MLZ372 | |
F | MLZ372 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000269|PubMed:10656795 |
Chain | Residue | Details |
B | LYS373 | |
E | TYR335 | |
F | LYS373 | |
A | THR266 | |
A | LYS317 | |
A | TYR335 | |
E | TYR245 | |
E | ASP256 | |
E | THR266 | |
E | LYS317 |
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 |
E | TYR245 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
E | HIS293 | electrostatic stabiliser, hydrogen bond acceptor |
E | HIS297 | electrostatic stabiliser, hydrogen bond acceptor |
E | TYR305 | activator, electrostatic stabiliser, hydrogen bond acceptor |
E | TYR335 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |