6KDS: Human NRMT2

Crystal structure of human NRMT2 in complex with alpha-N-monomethylated human CENP-A peptide. Determined by X-ray diffraction at 1.84 Å resolution. Released 8 Jul 2020.

Method
X-ray diffraction
Resolution
1.84 Å
Organism
Homo sapiens
Chains
2
Atoms
2,019
Mol. weight
28.65 kDa
Ligands
SAH
Released
8 Jul 2020

Explore 6KDS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6KDS contains 15 α-helices and 15 β-strands across 2 chains. 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: 15 helices, 14 β-strands

ElementResiduesLengthSheet
α-helix65-7713
α-helix83-875
α-helix91-933
α-helix94-10815
β-strand10911
β-strand11511
β-strand119-12352
α-helix129-1302
α-helix131-1355
β-strand141-14662
α-helix149-15810
α-helix160-1656
β-strand166-17162
α-helix174-1763
α-helix179-1802
β-strand184-19072
α-helix193-1953
α-helix198-21013
β-strand212-223122
β-strand22513
β-strand230-23234
β-strand237-23934
β-strand24113
α-helix242-25110
β-strand256-26162
α-helix262-2632
β-strand26915
α-helix270-2712
β-strand272-27762
Chain E: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand415

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Alpha N-terminal protein methyltransferase 1BAprotein244Homo sapiensQ5VVY1 (AlphaFold model)
CENP-A peptideEprotein6Homo sapiensP49450 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6KDS_1 Alpha N-terminal protein methyltransferase 1B (chains A)
MGSSHHHHHHSSGLVPRGSHMVINGEMQFYARAKLFYQEVPATEEGMMGNFIELSSPDIQ
ASQKFLRKFVGGPGRAGTDCALDCGSGIGRVSKHVLLPVFNSVELVDMMESFLLEAQNYL
QVKGDKVESYHCYSLQEFTPPFRRYDVIWIQWVSGHLTDKDLLAFLSRCRDGLKENGIII
LKDNVAREGCILDLSDSSVTRDMDILRSLIRKSGLVVLGQEKQDGFPEQCIPVWMFALHS
DRHS
Sequence of entity 2 (E), FASTA
>6KDS_2 CENP-A peptide (chains E)
GPRRRS

Ligands and cofactors

IDNameFormulaCopies
SAHS-adenosyl-L-homocysteineC14 H20 N6 O5 S1

Primary citation

Substrate engagement regulates state-specific alpha-N methylation of CENP-A by NRMT2. Wu, R., Yue, Y., Zheng, X. et al. To be published.

Other PDB entries of the same protein (UniProt Q5VVY1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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