4W5A: Complex structure of ATRX ADD

Complex structure of ATRX ADD bound to H3K9me3S10ph peptide. Determined by X-ray diffraction at 2.6 Å resolution. Released 21 Jan 2015.

Method

X-ray diffraction

Resolution

2.6 Å

Chains

6

Atoms

3,229

Mol. weight

50.03 kDa

Released

21 Jan 2015

Explore 4W5A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4W5A contains 19 α-helices and 28 β-strands across 6 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: 6 helices, 8 β-strands

Chain B: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	10	1	5
β-strand	17	1	5
β-strand	26-28	3	6
β-strand	35-37	3	6
α-helix	38-44	7
α-helix	48-50	3
β-strand	51	1	7
β-strand	57	1	7
β-strand	60	1	8
β-strand	68-71	4	8
β-strand	78-80	3	8
α-helix	81-87	7
α-helix	90-96	7
α-helix	102-104	3
α-helix	111-113	3
α-helix	114-125	12

Chains C, D and F: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	2-5	4	4

Chain E: 6 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	9-10	2	9
β-strand	17-18	2	9
β-strand	27-28	2	10
β-strand	35-36	2	10
α-helix	38-44	7
α-helix	48-50	3
β-strand	51	1	11
β-strand	57	1	11
β-strand	68-71	4	12
β-strand	78-80	3	12
α-helix	81-97	17
α-helix	102-104	3
α-helix	111-113	3
α-helix	114-126	13

Primary citation

ATRX tolerates activity-dependent histone H3 methyl/phos switching to maintain repetitive element silencing in neurons. Noh, K.M., Maze, I., Zhao, D. et al. Proc Natl Acad Sci U S A (2015) 112:6820-6827. DOI 10.1073/pnas.1411258112 · PubMed

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