5CHL: PDB entry 5CHL

Name: PDB 5CHL: Structural basis of H2A.Z recognition by YL1 histone chaperone component of SRCAP/SWR1 chromatin remodeling complex
Published: 2016-03-09
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Structural basis of H2A.Z recognition by YL1 histone chaperone component of SRCAP/SWR1 chromatin remodeling complex. Determined by X-ray diffraction at 1.89 Å resolution. Released 9 Mar 2016.

Method: X-ray diffraction
Resolution: 1.89 Å
Organisms: Drosophila melanogaster, Homo sapiens
Chains: 2
Atoms: 2,064
Mol. weight: 29.75 kDa
Released: 9 Mar 2016

Explore 5CHL in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5CHL contains 16 α-helices and 6 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: 5 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	17-32	16
α-helix	33-35	3
α-helix	44	1
β-strand	45	1	1
α-helix	46	1
α-helix	55-57	3

Chain B: 11 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	7-17	11
β-strand	22-23	2	2
β-strand	24	1	1
α-helix	25-50	26
β-strand	58	1	3
α-helix	60-70	11
α-helix	73-93	21
α-helix	103-113	11
α-helix	119	1
β-strand	120	1	3
α-helix	121	1
α-helix	122-144	23
α-helix	151-152	2
β-strand	154-155	2	2
α-helix	157-165	9
α-helix	168-178	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Vacuolar protein sorting-associated protein 72 homolog	A	protein	74	Drosophila melanogaster	Q9VKM6 (AlphaFold model)
Histone H2A.Z	B	protein	193	Homo sapiens	P0C0S5 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5CHL_1 Vacuolar protein sorting-associated protein 72 homolog (chains A)
AASRSRRNNAGNKIAHLLNEEEEDDFYKTSYGGFQEDEEDKEYEQKDEEEDVVDSDFSID
ENDEPVSDQEEAPE

Sequence of entity 2 (B), FASTA

>5CHL_2 Histone H2A.Z (chains B)
MRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITS
REIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSKQRAGLQFPVGRIHRHLKSRTTSHGRV
GATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAG
GGVIPHLVPRGSH

Primary citation

Structural basis of H2A.Z recognition by SRCAP chromatin-remodeling subunit YL1. Liang, X., Shan, S., Pan, L. et al. Nat Struct Mol Biol (2016) 23:317-323. DOI 10.1038/nsmb.3190 · PubMed

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