3QWW
Crystal structure of histone lysine methyltransferase SmyD2 in complex with the methyltransferase inhibitor sinefungin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
| A | 0000993 | molecular_function | RNA polymerase II complex binding |
| A | 0002039 | molecular_function | p53 binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006325 | biological_process | chromatin organization |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0007507 | biological_process | heart development |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008285 | biological_process | negative regulation of cell population proliferation |
| A | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| A | 0018026 | biological_process | peptidyl-lysine monomethylation |
| A | 0018027 | biological_process | peptidyl-lysine dimethylation |
| A | 0032259 | biological_process | methylation |
| A | 0042054 | molecular_function | histone methyltransferase activity |
| A | 0043516 | biological_process | regulation of DNA damage response, signal transduction by p53 class mediator |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046975 | molecular_function | histone H3K36 methyltransferase activity |
| A | 0140999 | molecular_function | histone H3K4 trimethyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE SFG A 434 |
| Chain | Residue |
| A | GLY16 |
| A | ASN206 |
| A | HIS207 |
| A | TYR240 |
| A | TYR258 |
| A | PHE260 |
| A | HOH452 |
| A | HOH454 |
| A | HOH473 |
| A | HOH493 |
| A | HOH544 |
| A | LYS17 |
| A | HOH557 |
| A | HOH866 |
| A | ARG19 |
| A | GLU135 |
| A | HIS137 |
| A | CYS181 |
| A | ASN182 |
| A | ALA203 |
| A | LEU204 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 435 |
| Chain | Residue |
| A | CYS52 |
| A | CYS55 |
| A | CYS74 |
| A | CYS78 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 436 |
| Chain | Residue |
| A | CYS65 |
| A | CYS68 |
| A | HIS86 |
| A | CYS90 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 437 |
| Chain | Residue |
| A | CYS209 |
| A | CYS262 |
| A | CYS264 |
| A | CYS267 |
Functional Information from PROSITE/UniProt
| site_id | PS01360 |
| Number of Residues | 41 |
| Details | ZF_MYND_1 Zinc finger MYND-type signature. HhcecCfarkeglsk........CgrCkqafYCdveCqkedwpl..Hkle.C |
| Chain | Residue | Details |
| A | HIS50-CYS90 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 38 |
| Details | ZN_FING: MYND-type => ECO:0000255|PROSITE-ProRule:PRU00134 |
| Chain | Residue | Details |
| A | CYS52-CYS90 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS17 | |
| A | ASN206 | |
| A | TYR258 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00134 |
| Chain | Residue | Details |
| A | CYS52 | |
| A | CYS55 | |
| A | CYS65 | |
| A | CYS68 | |
| A | CYS74 | |
| A | CYS78 | |
| A | HIS86 | |
| A | CYS90 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00190 |
| Chain | Residue | Details |
| A | HIS137 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9NRG4 |
| Chain | Residue | Details |
| A | SER283 |
