Brand  (β version)

PDB ID: 4FMU

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show 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
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

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: EC: Evidence:
Physiological Direction:
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 2.1.1.359 PubMed:19332550, PubMed:23043551, PubMed:27474439
-
L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)- methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine - PubMed:23043551, PubMed:28753426
-
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 - PubMed:27518565
-