4PLL: Chromodaomain of MRG2

Structure of the chromodaomain of MRG2 in complex with H3K36me3. Determined by X-ray diffraction at 2.6 Å resolution. Released 22 Jul 2015.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Arabidopsis thaliana
Chains: 4
Atoms: 1,028
Mol. weight: 20.76 kDa
Released: 22 Jul 2015

Explore 4PLL in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4PLL contains 3 α-helices and 10 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: 2 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	57-62	6	1
β-strand	65-77	13	1
β-strand	80-87	8	1
α-helix	92-94	3
β-strand	96-98	3	1
α-helix	100-102	3
β-strand	103-105	3	1

Chain B: 1 helix, 5 β-strands

Element	Residues	Length	Sheet
β-strand	57-62	6	1
β-strand	65-77	13	1
β-strand	80-87	8	1
β-strand	96-98	3	1
α-helix	100-102	3
β-strand	103-104	2	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
At1g02740	A, B	protein	75	Arabidopsis thaliana	Q4V3E2 (AlphaFold model)
H3K36me3	C, D	protein	11	Arabidopsis thaliana	P59169 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4PLL_1 At1g02740 (chains A, B)
GSHFEEGERVLAKHSDCFYEAKVLKVEFKDNEWKYFVHYIGWNKSWDEWIRLDCLLKHSD
ENIEKQKEQGLKQQG

Sequence of entity 2 (C, D), FASTA

>4PLL_2 H3K36me3 (chains C, D)
ATGGVKKPHRY

Primary citation

Regulation of arabidopsis flowering by the histone mark readers MRG1/2 via interaction with CONSTANS to modulate FT expression. Bu, Z., Yu, Y., Li, Z. et al. PLoS Genet (2014) 10:e1004617-e1004617. DOI 10.1371/journal.pgen.1004617 · PubMed

Other PDB entries of the same protein (UniProt Q4V3E2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4PLI 1.65 Å, Structure of the chromodomain of MRG2 in complex with H3K36me3
4PL6 1.68 Å, Structure of the chromodomain of MRG2 in complex with H3K4me3

Browse structure collections

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