4CAY: Human Anp32e-H2A.Z-H2B complex

Crystal structure of a human Anp32e-H2A.Z-H2B complex. Determined by X-ray diffraction at 1.48 Å resolution. Released 22 Jan 2014.

Method: X-ray diffraction
Resolution: 1.48 Å
Organism: HOMO SAPIENS
Chains: 3
Atoms: 1,829
Mol. weight: 26.4 kDa
Released: 22 Jan 2014

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

Secondary structure: helices and β-sheets

4CAY contains 12 α-helices and 6 β-strands across 3 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, 2 β-strands

Element	Residues	Length	Sheet
α-helix	19-22	4
α-helix	29-38	10
β-strand	46	1	1
α-helix	48-75	28
β-strand	80-81	2	2
α-helix	83-91	9
α-helix	94-105	12

Chain B: 4 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	38-48	11
β-strand	53-54	2	2
β-strand	55	1	3
α-helix	56-82	27
β-strand	89	1	1
α-helix	91-101	11
α-helix	104-123	20

Chain C: 3 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	218-222	5
α-helix	233	1
β-strand	234	1	3
α-helix	235	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone H2A.Z	A	protein	111	HOMO SAPIENS	P0C0S5 (AlphaFold model)
Histone H2B type 1-J	B	protein	97	HOMO SAPIENS	P06899 (AlphaFold model)
Acidic leucine-rich nuclear phosphoprotein 32 family member E	C	protein	30	HOMO SAPIENS	Q9BTT0 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4CAY_1 HISTONE H2A.Z (chains A)
MSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDL
KVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV

Sequence of entity 2 (B), FASTA

>4CAY_2 HISTONE H2B TYPE 1-J (chains B)
MKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRST
ITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK

Sequence of entity 3 (C), FASTA

>4CAY_3 ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN 32 FAMILY MEMBER E (chains C)
GSHMEVGLSYLMKEEIQDEEDDDDYVEEGE

Primary citation

Anp32E is a Histone Chaperone that Removes H2A.Z from Chromatin. Obri, A., Ouararhni, K., Papin, C. et al. Nature (2014) 648:505. DOI 10.1038/NATURE12922 · PubMed

Other PDB entries of the same protein (UniProt P0C0S5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6KO2 1.5 Å, Crystal Structure of BRD4-Brmo2 in complex with H2A.ZK4acK7ac peptide
5CHL 1.89 Å, Structural basis of H2A.Z recognition by YL1 histone chaperone component of SRCAP/SWR1…
9INC 2.01 Å, High resolutional Crystal Structure of human H2A.Z-H2B dimer in complex with human YL1-Z…
6JOU 2.17 Å, Crystal structure of the human nucleosome containing H2A.Z.1 S42R
5B31 2.2 Å, The crystal structure of the heterotypic H2AZ/H2A nucleosome with H3.1.
5B32 2.35 Å, The crystal structure of the heterotypic H2AZ/H2A nucleosome with H3.3.
5Z30 2.45 Å, The crystal structure of the nucleosome containing a cancer-associated histone H2A.Z…
9UBD 2.53 Å, The Structural Basis of the Recognition of the Histone Variant H2A.Z by the SRCAP…
1F66 2.6 Å, 2.6 a crystal structure of a nucleosome core particle containing the variant histone H2A.Z
8T9F 2.6 Å, Catalytic and non-catalytic mechanisms of histone H4 lysine 20 methyltransferase SUV420H1
4NFT 2.61 Å, Crystal structure of human lnkH2B-h2A.Z-Anp32e
5FUG 2.7 Å, Crystal structure of a human YL1-H2A.Z-H2B complex

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