6PAF
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 | 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 | HOH812 |
A | HOH822 |
A | HOH832 |
A | HOH901 |
A | HOH1044 |
A | HOH1049 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue MG A 505 |
Chain | Residue |
A | HOH656 |
A | HOH719 |
A | HOH724 |
A | HOH767 |
A | HOH794 |
A | HOH974 |
site_id | AC6 |
Number of Residues | 9 |
Details | binding site for residue GOL A 506 |
Chain | Residue |
A | ASP332 |
A | ASP336 |
A | TYR358 |
A | VAL368 |
A | VAL371 |
A | GLN372 |
A | LYS375 |
A | HOH632 |
A | HOH996 |
site_id | AC7 |
Number of Residues | 10 |
Details | binding site for residue GOL A 507 |
Chain | Residue |
A | SER213 |
A | ILE214 |
A | CYS238 |
A | HIS366 |
A | PRO367 |
A | O6A509 |
A | HOH639 |
A | HOH705 |
A | HOH713 |
A | HOH739 |
site_id | AC8 |
Number of Residues | 24 |
Details | binding site for residue SAM A 508 |
Chain | Residue |
A | ARG14 |
A | GLY15 |
A | ASN16 |
A | TYR124 |
A | GLU130 |
A | ASN132 |
A | CYS180 |
A | ASN181 |
A | SER202 |
A | LEU203 |
A | LEU204 |
A | ASN205 |
A | HIS206 |
A | TYR239 |
A | TYR257 |
A | PHE259 |
A | O6A509 |
A | HOH655 |
A | HOH672 |
A | HOH722 |
A | HOH742 |
A | HOH776 |
A | HOH835 |
A | HOH852 |
site_id | AC9 |
Number of Residues | 20 |
Details | binding site for residue O6A A 509 |
Chain | Residue |
A | CYS180 |
A | ASN181 |
A | SER182 |
A | PHE183 |
A | THR184 |
A | CYS186 |
A | MET190 |
A | ILE237 |
A | TYR239 |
A | TYR257 |
A | HIS366 |
A | VAL368 |
A | GOL507 |
A | SAM508 |
A | HOH632 |
A | HOH639 |
A | HOH798 |
A | HOH836 |
A | HOH886 |
A | HOH996 |
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 | CYS49 | |
A | CYS52 | |
A | CYS62 | |
A | CYS65 | |
A | CYS71 | |
A | CYS75 | |
A | HIS83 | |
A | CYS87 |
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 |