Brand  (β version)

PDB ID: 4FMU

Hetero Atom Contents

color scheme of protein:

hetatm:

x
information
centroid:
interaction residue:

chain:

Ligands
Code Name Link
0UM (2s,5s)-2-amino-6-[(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]-5-(propylamino)hexanoic acid PoSSuM
UNX Unknown atom or ion PoSSuM
ZN Zinc ion PoSSuM

Structure summary

Code : 4FMU   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Crystal structure of Methyltransferase domain of human SET domain-containing protein 2 Compound: Pr-SNF
Release Data : 2012-09-05
Compound :
mol_id molecule chains synonym
1 Histone-lysine N-methyltransferase SETD2 A HIF-1, Huntingtin yeast partner B, Huntingtin-interacting protein 1, HIP-1, Huntingtin-interacting protein B, Lysine N-methyltransferase 3A, SET domain-containing protein 2, hSET2, p231HBP
ec: 2.1.1.43
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: SETD2, HIF1, HYPB, KIAA1732, KMT3A, SET2, HSPC069
expression_system_strain: BL21 (DE3)V2RpRARE
expression_system_vector_type: PLASMID
expression_system_plasmid: pET28-MHL
Authors : Dong, A., Zeng, H., Ibanez, G., Zheng, W., Tempel, W., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Brown, P.J., Min, J., Luo, M., Wu, H., Structural Genomics Consortium (SGC)
Keywords : Structural Genomics Consortium, SGC, Methyltransferase, SET domain-containing protein 2, Pr-SNF, transferase
Exp. method : X-RAY DIFFRACTION ( 2.10 Å )
Citation :

Sinefungin Derivatives as Inhibitors and Structure Probes of Protein Lysine Methyltransferase SETD2.

Zheng, W.,Ibanez, G.,Wu, H.  et al.
(2012)  J.Am.Chem.Soc.  134 : 18004 - 18014

PubMed: 23043551
DOI: 10.1021/ja307060p

Reaction

Chain : A
UniProt : Q9BYW2 (SETD2_HUMAN)
Reaction : Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L- homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA- COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359; Evidence={ECO:0000269|PubMed:19332550, ECO:0000269|PubMed:23043551, ECO:0000269|PubMed:27474439};
Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)- methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence={ECO:0000269|PubMed:23043551, ECO:0000269|PubMed:28753426};
Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L- homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA- COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; Evidence={ECO:0000269|PubMed:27518565};