3OXF
Human lysine methyltransferase Smyd3 in complex with AdoHcy (Form I)
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 |
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 | 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 | 14 |
Details | BINDING SITE FOR RESIDUE SAH A 437 |
Chain | Residue |
A | ARG14 |
A | HIS206 |
A | TYR239 |
A | TYR257 |
A | PHE259 |
A | HOH450 |
A | GLY15 |
A | ASN16 |
A | TYR124 |
A | GLU130 |
A | ASN132 |
A | ASN181 |
A | SER202 |
A | ASN205 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 438 |
Chain | Residue |
A | CYS49 |
A | CYS52 |
A | CYS71 |
A | CYS75 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 439 |
Chain | Residue |
A | CYS62 |
A | CYS65 |
A | HIS83 |
A | CYS87 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 440 |
Chain | Residue |
A | CYS208 |
A | CYS261 |
A | CYS263 |
A | CYS266 |
site_id | AC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE SAH B 437 |
Chain | Residue |
B | ARG14 |
B | GLY15 |
B | ASN16 |
B | TYR124 |
B | ASN132 |
B | SER202 |
B | LEU204 |
B | ASN205 |
B | HIS206 |
B | TYR239 |
B | TYR257 |
B | PHE259 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 438 |
Chain | Residue |
B | CYS49 |
B | CYS52 |
B | CYS71 |
B | CYS75 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 439 |
Chain | Residue |
B | CYS62 |
B | CYS65 |
B | HIS83 |
B | CYS87 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 440 |
Chain | Residue |
B | CYS208 |
B | CYS261 |
B | CYS263 |
B | CYS266 |
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 | |
A | CYS52 | |
A | CYS62 | |
A | CYS65 | |
A | CYS71 | |
B | CYS49 | |
B | CYS52 | |
B | CYS62 | |
B | CYS65 | |
B | CYS71 | |
B | CYS75 | |
B | HIS83 | |
B | CYS87 | |
A | CYS75 | |
A | HIS83 | |
A | CYS87 |
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 | |
A | ASN132 | |
A | ASN181 | |
A | TYR239 | |
A | PHE259 | |
B | TYR124 | |
B | ASN132 | |
B | ASN181 | |
B | TYR239 | |
B | PHE259 |
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 |