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7LMS

Structure of human SetD3 methyl-transferase in complex with 2A protease from Coxsackievirus B3

Functional Information from GO Data
ChainGOidnamespacecontents
A0000785cellular_componentchromatin
A0003713molecular_functiontranscription coactivator activity
A0003779molecular_functionactin binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0006338biological_processchromatin remodeling
A0008168molecular_functionmethyltransferase activity
A0008170molecular_functionN-methyltransferase activity
A0008276molecular_functionprotein methyltransferase activity
A0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
A0016279molecular_functionprotein-lysine N-methyltransferase activity
A0018021biological_processpeptidyl-histidine methylation
A0018023biological_processpeptidyl-lysine trimethylation
A0018064molecular_functionprotein-L-histidine N-tele-methyltransferase activity
A0030047biological_processactin modification
A0032259biological_processmethylation
A0042800molecular_functionhistone H3K4 methyltransferase activity
A0045893biological_processpositive regulation of DNA-templated transcription
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046975molecular_functionhistone H3K36 methyltransferase activity
A0051149biological_processpositive regulation of muscle cell differentiation
A0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
A0070472biological_processregulation of uterine smooth muscle contraction
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016032biological_processviral process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:30626964, ECO:0000269|PubMed:30785395, ECO:0000269|PubMed:31388018, ECO:0000269|PubMed:31911441, ECO:0000269|PubMed:31993215, ECO:0000269|PubMed:32503840, ECO:0000269|Ref.12, ECO:0007744|PDB:3SMT, ECO:0007744|PDB:6ICT, ECO:0007744|PDB:6ICV, ECO:0007744|PDB:6JAT, ECO:0007744|PDB:6MBJ, ECO:0007744|PDB:6MBK, ECO:0007744|PDB:6MBL, ECO:0007744|PDB:6OX0, ECO:0007744|PDB:6OX1, ECO:0007744|PDB:6OX2, ECO:0007744|PDB:6OX3, ECO:0007744|PDB:6OX4, ECO:0007744|PDB:6OX5, ECO:0007744|PDB:6V62, ECO:0007744|PDB:6V63, ECO:0007744|PDB:6WK1, ECO:0007744|PDB:6WK2
ChainResidueDetails
AARG75
AGLU104
AARG254
AASP275
ASER325

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER513
BCYS55
BCYS113
BHIS115

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Cleavage; by protease 3C => ECO:0000250|UniProtKB:P03301
ChainResidueDetails
BGLN147

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PDB entries from 2024-07-24

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