PDB Information

PDB3OXF
MethodX-RAY DIFFRACTION
Host OrganismEscherichia coli
Gene SourceHomo sapiens
Primary Citation
Structural and biochemical studies of human lysine methyltransferase Smyd3 reveal the important functional roles of its post-SET and TPR domains and the regulation of its activity by DNA binding.
Xu, S., Wu, J., Sun, B., Zhong, C., Ding, J.
Nucleic Acids Res.
HeaderTransferase
Released2010-09-21
Resolution2.820
CATH Insert Date27 Feb, 2011

PDB Images (13)

PDB Prints

PDB Chains (2)

Chain ID Date inserted into CATH CATH Status
A 28 Feb, 2011 Chopped
B 28 Feb, 2011 Chopped

CATH Domains (10)

Domain ID Date inserted into CATH Superfamily CATH Status
3oxfA01 10 Oct, 2013 2.170.270.10 Assigned
3oxfA02 10 Oct, 2013 6.10.140.2220 Assigned
3oxfA03 10 Oct, 2013 1.10.220.160 Assigned
3oxfA04 10 Oct, 2013 1.25.40.970 Assigned
3oxfA05 10 Oct, 2013 1.25.40.10 Assigned
3oxfB01 10 Oct, 2013 2.170.270.10 Assigned
3oxfB02 10 Oct, 2013 6.10.140.2220 Assigned
3oxfB03 10 Oct, 2013 1.10.220.160 Assigned
3oxfB04 10 Oct, 2013 1.25.40.970 Assigned
3oxfB05 10 Oct, 2013 1.25.40.10 Assigned

UniProtKB Entries (2)

Accession Gene ID Taxon Description
Q9H7B4 SMYD3_HUMAN Homo sapiens Histone-lysine N-methyltransferase SMYD3
Q9H7B4 SMYD3_HUMAN Homo sapiens Histone-lysine N-methyltransferase SMYD3
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