3S7D
Structural Basis of Substrate Methylation and Inhibition of SMYD2
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 | 0005654 | cellular_component | nucleoplasm |
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 | 0016278 | molecular_function | lysine N-methyltransferase activity |
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 | 0140938 | molecular_function | histone H3 methyltransferase activity |
A | 0140999 | molecular_function | histone H3K4 trimethyltransferase activity |
A | 1901796 | biological_process | regulation of signal transduction by p53 class mediator |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE SAH A 1000 |
Chain | Residue |
A | GLY16 |
A | LEU204 |
A | ASN206 |
A | HIS207 |
A | TYR240 |
A | TYR258 |
A | PHE260 |
A | HOH445 |
A | HOH455 |
A | HOH480 |
A | HOH482 |
A | LYS17 |
I | MLZ370 |
A | ARG19 |
A | GLU135 |
A | HIS137 |
A | LYS162 |
A | CYS181 |
A | ASN182 |
A | ALA203 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BU3 A 434 |
Chain | Residue |
A | TRP356 |
A | GLY394 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BU3 A 435 |
Chain | Residue |
A | ASP242 |
A | LEU244 |
A | TYR245 |
A | HIS341 |
A | TYR344 |
A | TYR370 |
A | TYR374 |
I | LYS373 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE BU3 A 436 |
Chain | Residue |
A | THR44 |
A | GLU104 |
A | HIS193 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 437 |
Chain | Residue |
A | CYS52 |
A | CYS55 |
A | CYS74 |
A | CYS78 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 438 |
Chain | Residue |
A | CYS65 |
A | CYS68 |
A | HIS86 |
A | CYS90 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 439 |
Chain | Residue |
A | CYS209 |
A | CYS262 |
A | CYS264 |
A | CYS267 |
Functional Information from PROSITE/UniProt
site_id | PS01360 |
Number of Residues | 40 |
Details | ZF_MYND_1 Zinc finger MYND-type signature. Hcey.Cftrkeglsk........CgrCkqafYCnveCqkedwpm..Hkle.C |
Chain | Residue | Details |
A | HIS51-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: |
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, ECO:0000269|PubMed:21724641 |
Chain | Residue | Details |
A | HIS137 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER283 |