4E47
SET7/9 in complex with inhibitor (R)-(3-(3-cyanophenyl)-1-oxo-1-(pyrrolidin-1-yl)propan-2-yl)-1,2,3,4-tetrahydroisoquinoline-6- sulfonamide and S-adenosylmethionine
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 |
| C | 0005694 | cellular_component | chromosome |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| C | 0140945 | molecular_function | histone H3K4 monomethyltransferase activity |
| D | 0005694 | cellular_component | chromosome |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| D | 0140945 | molecular_function | histone H3K4 monomethyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE SAM A 401 |
| Chain | Residue |
| A | ALA226 |
| A | TYR335 |
| A | TRP352 |
| A | HOH522 |
| A | HOH530 |
| A | HOH597 |
| A | HOH598 |
| A | HOH603 |
| A | HOH625 |
| A | HOH632 |
| A | GLU228 |
| A | GLY264 |
| A | ASN265 |
| A | HIS293 |
| A | LYS294 |
| A | ALA295 |
| A | ASN296 |
| A | HIS297 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 0N6 A 402 |
| Chain | Residue |
| A | TYR245 |
| A | HIS252 |
| A | ASP256 |
| A | ASN263 |
| A | GLY264 |
| A | THR266 |
| A | LEU267 |
| A | SER268 |
| A | TYR305 |
| A | TYR335 |
| A | GLY336 |
| A | TYR337 |
| A | HOH513 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME A 403 |
| Chain | Residue |
| A | CYS200 |
| A | SER202 |
| A | HOH506 |
| D | GLU351 |
| D | GLN354 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 404 |
| Chain | Residue |
| A | TYR122 |
| A | HOH512 |
| A | HOH741 |
| B | TRP120 |
| B | TYR122 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE SAM B 800 |
| Chain | Residue |
| B | ALA226 |
| B | GLU228 |
| B | GLY264 |
| B | ASN265 |
| B | HIS293 |
| B | LYS294 |
| B | ALA295 |
| B | ASN296 |
| B | HIS297 |
| B | TYR335 |
| B | TRP352 |
| B | HOH930 |
| B | HOH969 |
| B | HOH972 |
| B | HOH985 |
| B | HOH988 |
| B | HOH1014 |
| B | HOH1038 |
| B | HOH1058 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 0N6 B 801 |
| Chain | Residue |
| B | TYR245 |
| B | HIS252 |
| B | ASP256 |
| B | ASN263 |
| B | GLY264 |
| B | THR266 |
| B | LEU267 |
| B | SER268 |
| B | TYR305 |
| B | TYR335 |
| B | GLY336 |
| B | TYR337 |
| B | HOH966 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE SAM C 800 |
| Chain | Residue |
| C | ALA226 |
| C | GLU228 |
| C | GLY264 |
| C | ASN265 |
| C | HIS293 |
| C | LYS294 |
| C | ALA295 |
| C | ASN296 |
| C | HIS297 |
| C | TYR335 |
| C | TRP352 |
| C | HOH937 |
| C | HOH949 |
| C | HOH962 |
| C | HOH977 |
| C | HOH1015 |
| C | HOH1056 |
| C | HOH1057 |
| C | HOH1071 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 0N6 C 801 |
| Chain | Residue |
| C | LEU267 |
| C | SER268 |
| C | TYR305 |
| C | TYR335 |
| C | GLY336 |
| C | TYR337 |
| C | HIS339 |
| C | HOH989 |
| C | TYR245 |
| C | HIS252 |
| C | ASP256 |
| C | TRP260 |
| C | ASN263 |
| C | GLY264 |
| C | THR266 |
| site_id | AC9 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE SAM D 800 |
| Chain | Residue |
| D | ALA226 |
| D | GLU228 |
| D | GLY264 |
| D | ASN265 |
| D | HIS293 |
| D | LYS294 |
| D | ALA295 |
| D | ASN296 |
| D | HIS297 |
| D | TYR335 |
| D | TRP352 |
| D | HOH910 |
| D | HOH964 |
| D | HOH1011 |
| D | HOH1055 |
| D | HOH1059 |
| D | HOH1071 |
| site_id | BC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 0N6 D 801 |
| Chain | Residue |
| D | TYR245 |
| D | HIS252 |
| D | ASP256 |
| D | TRP260 |
| D | ASN263 |
| D | GLY264 |
| D | THR266 |
| D | LEU267 |
| D | SER268 |
| D | TYR305 |
| D | TYR335 |
| D | GLY336 |
| D | TYR337 |
| D | HOH927 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12514135, ECO:0000269|PubMed:12540855 |
| Chain | Residue | Details |
| A | ALA226 | |
| D | ALA226 | |
| D | ASN296 | |
| D | HIS297 | |
| A | ASN296 | |
| A | HIS297 | |
| B | ALA226 | |
| B | ASN296 | |
| B | HIS297 | |
| C | ALA226 | |
| C | ASN296 | |
| C | HIS297 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00190, ECO:0000269|PubMed:12514135, ECO:0000269|PubMed:12540855 |
| Chain | Residue | Details |
| A | GLU356 | |
| B | GLU356 | |
| C | GLU356 | |
| D | GLU356 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | SITE: Histone H3K4 binding => ECO:0000269|PubMed:12540855 |
| Chain | Residue | Details |
| A | TYR245 | |
| B | TYR335 | |
| C | TYR245 | |
| C | ASP256 | |
| C | THR266 | |
| C | LYS317 | |
| C | TYR335 | |
| D | TYR245 | |
| D | ASP256 | |
| D | THR266 | |
| D | LYS317 | |
| A | ASP256 | |
| D | TYR335 | |
| A | THR266 | |
| A | LYS317 | |
| A | TYR335 | |
| B | TYR245 | |
| B | ASP256 | |
| B | THR266 | |
| B | LYS317 |
Catalytic Information from CSA
| 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 |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 350 |
| Chain | Residue | Details |
| C | TYR245 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| C | HIS293 | electrostatic stabiliser, hydrogen bond acceptor |
| C | HIS297 | electrostatic stabiliser, hydrogen bond acceptor |
| C | TYR305 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| C | TYR335 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 350 |
| Chain | Residue | Details |
| D | TYR245 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| D | HIS293 | electrostatic stabiliser, hydrogen bond acceptor |
| D | HIS297 | electrostatic stabiliser, hydrogen bond acceptor |
| D | TYR305 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| D | TYR335 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
