5HQ8
Co-crystal Structure of human SMYD3 with a MEKK2 peptide at 2.13A
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 | 0016740 | molecular_function | transferase activity |
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 |
B | 0000978 | molecular_function | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
B | 0000993 | molecular_function | RNA polymerase II complex binding |
B | 0001162 | molecular_function | RNA polymerase II intronic transcription regulatory region sequence-specific DNA 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 | 0006334 | biological_process | nucleosome assembly |
B | 0008168 | molecular_function | methyltransferase activity |
B | 0014904 | biological_process | myotube cell development |
B | 0016740 | molecular_function | transferase activity |
B | 0032259 | biological_process | methylation |
B | 0033138 | biological_process | positive regulation of peptidyl-serine phosphorylation |
B | 0042054 | molecular_function | histone methyltransferase activity |
B | 0045184 | biological_process | establishment of protein localization |
B | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
B | 0046872 | molecular_function | metal ion binding |
B | 0071549 | biological_process | cellular response to dexamethasone stimulus |
B | 0140939 | molecular_function | histone H4 methyltransferase activity |
B | 0140954 | molecular_function | histone H3K36 dimethyltransferase activity |
B | 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 | 4 |
Details | binding site for residue MG A 504 |
Chain | Residue |
A | PRO167 |
A | PHE169 |
A | HOH873 |
A | HOH924 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | LEU344 |
A | HIS382 |
A | GLN383 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue EDO A 506 |
Chain | Residue |
A | CYS238 |
A | LEU240 |
A | MET242 |
A | HIS366 |
A | HOH710 |
I | GLY262 |
I | TYR264 |
site_id | AC7 |
Number of Residues | 23 |
Details | binding site for residue SAH A 507 |
Chain | Residue |
A | ARG14 |
A | GLY15 |
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 | HOH671 |
A | HOH698 |
A | HOH753 |
A | HOH789 |
A | HOH804 |
A | HOH865 |
A | HOH878 |
I | LYS260 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue ZN B 501 |
Chain | Residue |
B | CYS208 |
B | CYS261 |
B | CYS263 |
B | CYS266 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue ZN B 502 |
Chain | Residue |
B | CYS62 |
B | CYS65 |
B | HIS83 |
B | CYS87 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue ZN B 503 |
Chain | Residue |
B | CYS49 |
B | CYS52 |
B | CYS71 |
B | CYS75 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue MG B 504 |
Chain | Residue |
B | PRO167 |
B | PHE169 |
B | HOH766 |
B | HOH848 |
B | HOH852 |
B | HOH853 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue EDO B 505 |
Chain | Residue |
B | THR184 |
B | CYS186 |
B | ILE214 |
B | PHE216 |
B | HOH649 |
J | GLY261 |
J | GLY262 |
J | HOH401 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue GOL B 506 |
Chain | Residue |
B | GLN152 |
B | ILE159 |
B | ALA162 |
B | LEU171 |
B | HOH607 |
B | HOH616 |
B | HOH786 |
site_id | AD5 |
Number of Residues | 7 |
Details | binding site for residue EDO B 507 |
Chain | Residue |
B | CYS238 |
B | LEU240 |
B | MET242 |
B | HIS366 |
B | HOH762 |
J | GLY262 |
J | TYR264 |
site_id | AD6 |
Number of Residues | 20 |
Details | binding site for residue SAH B 508 |
Chain | Residue |
B | TYR239 |
B | TYR257 |
B | PHE259 |
B | HOH611 |
B | HOH638 |
B | HOH642 |
B | HOH716 |
B | HOH721 |
B | HOH763 |
J | LYS260 |
B | ARG14 |
B | ASN16 |
B | TYR124 |
B | ASN132 |
B | CYS180 |
B | ASN181 |
B | SER202 |
B | LEU204 |
B | ASN205 |
B | HIS206 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue EDO I 301 |
Chain | Residue |
A | GLU192 |
I | GLY261 |
I | HOH405 |
I | HOH406 |
I | HOH407 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue EDO J 301 |
Chain | Residue |
B | GLU192 |
J | GLY261 |
J | HOH405 |
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 | 76 |
Details | ZN_FING: MYND-type => ECO:0000255|PROSITE-ProRule:PRU00134 |
Chain | Residue | Details |
A | CYS49-CYS87 | |
B | CYS49-CYS87 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|Ref.12 |
Chain | Residue | Details |
A | ARG14 | |
A | ASN205 | |
B | ARG14 | |
B | ASN205 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00134 |
Chain | Residue | Details |
A | CYS49 | |
B | CYS52 | |
B | CYS62 | |
B | CYS65 | |
B | CYS71 | |
B | CYS75 | |
B | HIS83 | |
B | CYS87 | |
A | CYS52 | |
A | CYS62 | |
A | CYS65 | |
A | CYS71 | |
A | CYS75 | |
A | HIS83 | |
A | CYS87 | |
B | CYS49 |
site_id | SWS_FT_FI4 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00190, ECO:0000269|Ref.12 |
Chain | Residue | Details |
A | TYR124 | |
B | PHE259 | |
A | ASN132 | |
A | ASN181 | |
A | TYR239 | |
A | PHE259 | |
B | TYR124 | |
B | ASN132 | |
B | ASN181 | |
B | TYR239 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
A | MET1 | |
B | MET1 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR22 | |
B | THR22 |