3TG4
Structure of SMYD2 in complex with SAM
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 | 0008270 | molecular_function | zinc ion binding |
| 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 | 0016740 | molecular_function | transferase 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 | 18 |
| Details | BINDING SITE FOR RESIDUE SAM A 434 |
| Chain | Residue |
| A | GLY16 |
| A | HIS207 |
| A | TYR240 |
| A | TYR258 |
| A | PHE260 |
| A | GOL438 |
| A | HOH597 |
| A | HOH609 |
| A | HOH625 |
| A | HOH639 |
| A | LYS17 |
| A | ARG19 |
| A | HIS137 |
| A | CYS181 |
| A | ASN182 |
| A | ALA203 |
| A | LEU204 |
| A | ASN206 |
| 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 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 438 |
| Chain | Residue |
| A | CYS181 |
| A | ASN182 |
| A | GLY183 |
| A | PHE184 |
| A | ALA203 |
| A | TYR240 |
| A | TYR258 |
| A | SAM434 |
| A | GOL439 |
| A | HOH463 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 439 |
| Chain | Residue |
| A | PHE184 |
| A | THR185 |
| A | TYR240 |
| A | GOL438 |
| A | HOH535 |
| A | HOH561 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 440 |
| Chain | Residue |
| A | CYS209 |
| A | LEU243 |
| A | ARG250 |
| A | GLU266 |
| A | LYS272 |
| A | LYS276 |
| A | HIS373 |
| A | TYR374 |
| A | PRO375 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 441 |
| Chain | Residue |
| A | GLU190 |
| A | ARG390 |
| A | LEU391 |
| A | HOH617 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 442 |
| Chain | Residue |
| A | ALA38 |
| A | TYR39 |
| A | LYS115 |
| A | HOH596 |
| A | HOH624 |
| A | HOH648 |
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 | 234 |
| Details | Domain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 38 |
| Details | Zinc finger: {"description":"MYND-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00134","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00134","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21724641","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
