3RIB
Human lysine methyltransferase Smyd2 in complex with AdoHcy
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 | 0006351 | biological_process | DNA-templated transcription |
| 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 | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| 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 |
| B | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
| B | 0000993 | molecular_function | RNA polymerase II complex binding |
| B | 0002039 | molecular_function | p53 binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006325 | biological_process | chromatin organization |
| B | 0006338 | biological_process | chromatin remodeling |
| B | 0006351 | biological_process | DNA-templated transcription |
| B | 0007507 | biological_process | heart development |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008285 | biological_process | negative regulation of cell population proliferation |
| B | 0016278 | molecular_function | lysine N-methyltransferase activity |
| B | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0018026 | biological_process | peptidyl-lysine monomethylation |
| B | 0018027 | biological_process | peptidyl-lysine dimethylation |
| B | 0032259 | biological_process | methylation |
| B | 0042054 | molecular_function | histone methyltransferase activity |
| B | 0043516 | biological_process | regulation of DNA damage response, signal transduction by p53 class mediator |
| B | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0046975 | molecular_function | histone H3K36 methyltransferase activity |
| B | 0140938 | molecular_function | histone H3 methyltransferase activity |
| B | 0140999 | molecular_function | histone H3K4 trimethyltransferase activity |
| B | 1901796 | biological_process | regulation of signal transduction by p53 class mediator |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 442 |
| Chain | Residue |
| A | CYS52 |
| A | CYS55 |
| A | CYS74 |
| A | CYS78 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 443 |
| Chain | Residue |
| A | CYS65 |
| A | CYS68 |
| A | HIS86 |
| A | CYS90 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 444 |
| Chain | Residue |
| A | CYS262 |
| A | CYS264 |
| A | CYS267 |
| A | CYS209 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE SAH A 445 |
| Chain | Residue |
| A | GLY16 |
| A | LYS17 |
| A | ARG19 |
| A | GLU135 |
| A | HIS137 |
| A | CYS181 |
| A | ASN182 |
| A | ALA203 |
| A | LEU204 |
| A | ASN206 |
| A | HIS207 |
| A | TYR240 |
| A | TYR258 |
| A | PHE260 |
| A | SO4452 |
| A | HOH489 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 446 |
| Chain | Residue |
| A | HIS397 |
| A | ALA399 |
| A | ALA400 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 447 |
| Chain | Residue |
| A | CYS181 |
| A | GLY183 |
| A | PHE184 |
| A | TYR240 |
| A | TYR258 |
| A | SO4449 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 448 |
| Chain | Residue |
| A | THR105 |
| A | VAL179 |
| A | GLY183 |
| A | PHE184 |
| A | THR185 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 449 |
| Chain | Residue |
| A | GLY183 |
| A | THR185 |
| A | TYR240 |
| A | SO4447 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 450 |
| Chain | Residue |
| A | ASP252 |
| A | ARG253 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 451 |
| Chain | Residue |
| A | CYS209 |
| A | LEU243 |
| A | GLU266 |
| A | LYS272 |
| A | LYS276 |
| A | HIS373 |
| A | TYR374 |
| A | PRO375 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 452 |
| Chain | Residue |
| A | PRO15 |
| A | GLY16 |
| A | LYS17 |
| A | GLU263 |
| A | SAH445 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 442 |
| Chain | Residue |
| B | CYS52 |
| B | CYS55 |
| B | CYS74 |
| B | CYS78 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 443 |
| Chain | Residue |
| B | CYS65 |
| B | CYS68 |
| B | HIS86 |
| B | CYS90 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 444 |
| Chain | Residue |
| B | CYS209 |
| B | CYS262 |
| B | CYS264 |
| B | CYS267 |
| site_id | BC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SAH B 445 |
| Chain | Residue |
| B | GLY16 |
| B | LYS17 |
| B | ARG19 |
| B | GLU135 |
| B | HIS137 |
| B | CYS181 |
| B | ALA203 |
| B | ASN206 |
| B | HIS207 |
| B | TYR240 |
| B | TYR258 |
| B | PHE260 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 446 |
| Chain | Residue |
| B | GLY30 |
| B | LEU32 |
| B | ARG225 |
| B | GLY417 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 447 |
| Chain | Residue |
| B | HIS397 |
| B | LYS398 |
| B | ALA399 |
| B | ALA400 |
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 | 468 |
| Details | Domain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 76 |
| 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 | 10 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00134","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| 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 |
