2LV9: Histone-lysine N-methyltransferase MLL5

Solution NMR structure of the PHD domain of human MLL5, Northeast structural genomics consortium target HR6512A. Determined by solution NMR. Released 5 Sept 2012.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
645
Mol. weight
11.65 kDa
Ligands
ZN
Released
5 Sept 2012

Explore 2LV9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2LV9 contains 1 α-helix and 6 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 1 helix, 6 β-strands

ElementResiduesLengthSheet
β-strand11811
β-strand132-13432
β-strand13513
β-strand14011
β-strand141-14332
β-strand15813
α-helix170-18314

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone-lysine N-methyltransferase MLL5Aprotein98Homo sapiensQ8IZD2 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2LV9_1 Histone-lysine N-methyltransferase MLL5 (chains A)
MHHHHHHSSGRENLYFQGSEDGSYGTDVTRCICGFTHDDGYMICCDKCSVWQHIDCMGID
RQHIPDTYLCERCQPRNLDKERAVLLQRRKRENMSDGD

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

Primary citation

NMR solution structure of the human MLL5 PHD domain (CASP Target). Lemak, A., Yee, A., Houliston, S. et al. To be published.

Other PDB entries of the same protein (UniProt Q8IZD2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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