6P6G
Co-crystal Structure of human SMYD3 with Isoxazole Amides Inhibitors
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000978 | molecular_function | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
| A | 0000993 | molecular_function | RNA polymerase II complex binding |
| A | 0001162 | molecular_function | RNA polymerase II intronic transcription regulatory region sequence-specific DNA 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 | 0006334 | biological_process | nucleosome assembly |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0014904 | biological_process | myotube cell development |
| A | 0032259 | biological_process | methylation |
| A | 0033138 | biological_process | positive regulation of peptidyl-serine phosphorylation |
| A | 0042054 | molecular_function | histone methyltransferase activity |
| A | 0045184 | biological_process | establishment of protein localization |
| A | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071549 | biological_process | cellular response to dexamethasone stimulus |
| A | 0140939 | molecular_function | histone H4 methyltransferase activity |
| A | 0140954 | molecular_function | histone H3K36 dimethyltransferase activity |
| A | 0140999 | molecular_function | histone H3K4 trimethyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 501 |
| Chain | Residue |
| A | CYS208 |
| A | CYS261 |
| A | CYS263 |
| A | CYS266 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 502 |
| Chain | Residue |
| A | CYS62 |
| A | CYS65 |
| A | HIS83 |
| A | CYS87 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 503 |
| Chain | Residue |
| A | CYS52 |
| A | CYS71 |
| A | CYS75 |
| A | CYS49 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 504 |
| Chain | Residue |
| A | HOH696 |
| A | HOH741 |
| A | HOH786 |
| A | HOH811 |
| A | HOH966 |
| A | HOH969 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 505 |
| Chain | Residue |
| A | HOH632 |
| A | HOH643 |
| A | HOH653 |
| A | HOH670 |
| A | HOH681 |
| A | HOH871 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 506 |
| Chain | Residue |
| A | ASP332 |
| A | ASP336 |
| A | GLN372 |
| A | LYS375 |
| A | HOH684 |
| A | HOH808 |
| A | HOH823 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 507 |
| Chain | Residue |
| A | SER213 |
| A | ILE214 |
| A | CYS238 |
| A | HIS366 |
| A | PRO367 |
| A | LUP510 |
| A | HOH648 |
| A | HOH691 |
| A | HOH701 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 508 |
| Chain | Residue |
| A | PRO99 |
| A | MET113 |
| A | GLY115 |
| A | GLN146 |
| A | THR150 |
| A | HOH715 |
| site_id | AC9 |
| Number of Residues | 21 |
| Details | binding site for residue SAH A 509 |
| Chain | Residue |
| A | ARG14 |
| A | ASN16 |
| A | TYR124 |
| A | GLU130 |
| A | ASN132 |
| A | CYS180 |
| A | ASN181 |
| A | SER202 |
| A | LEU204 |
| A | ASN205 |
| A | HIS206 |
| A | TYR239 |
| A | TYR257 |
| A | PHE259 |
| A | HOH639 |
| A | HOH647 |
| A | HOH680 |
| A | HOH719 |
| A | HOH771 |
| A | HOH774 |
| A | HOH793 |
| site_id | AD1 |
| Number of Residues | 20 |
| Details | binding site for residue LUP A 510 |
| Chain | Residue |
| A | CYS180 |
| A | ASN181 |
| A | SER182 |
| A | PHE183 |
| A | THR184 |
| A | CYS186 |
| A | GLU192 |
| A | ILE237 |
| A | TYR239 |
| A | ASP241 |
| A | TYR257 |
| A | LEU290 |
| A | GLU294 |
| A | LYS329 |
| A | CYS333 |
| A | VAL368 |
| A | GOL507 |
| A | HOH602 |
| A | HOH759 |
| A | HOH810 |
Functional Information from PROSITE/UniProt
| site_id | PS01360 |
| Number of Residues | 39 |
| Details | ZF_MYND_1 Zinc finger MYND-type signature. Cdr..Cllgkeklmr........CsqCrvakYCsakCqkkawpd..Hkre.C |
| Chain | Residue | Details |
| A | CYS49-CYS87 |
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 | CYS49-CYS87 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|Ref.12 |
| Chain | Residue | Details |
| A | ARG14 | |
| A | ASN205 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00134 |
| Chain | Residue | Details |
| A | CYS71 | |
| A | CYS75 | |
| A | HIS83 | |
| A | CYS87 | |
| A | CYS49 | |
| A | CYS52 | |
| A | CYS62 | |
| A | CYS65 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00190, ECO:0000269|Ref.12 |
| Chain | Residue | Details |
| A | TYR124 | |
| A | ASN132 | |
| A | ASN181 | |
| A | TYR239 | |
| A | PHE259 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | MET1 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | THR22 |
