1ZR3: Histone macroH2A1.1

Crystal structure of the macro-domain of human core histone variant macroH2A1.1 (form B). Determined by X-ray diffraction at 1.66 Å resolution. Released 14 Feb 2006.

Method: X-ray diffraction
Resolution: 1.66 Å
Organism: Homo sapiens
Chains: 4
Atoms: 6,180
Mol. weight: 89.29 kDa
Released: 14 Feb 2006

Explore 1ZR3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1ZR3 contains 26 α-helices and 34 β-strands across 4 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: 8 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	185-190	6	1
α-helix	195	1
β-strand	196-201	6	1
α-helix	204-206	3
β-strand	211-216	6	1
α-helix	224-249	26
α-helix	252-253	2
β-strand	257-261	5	1
β-strand	269-274	6	1
α-helix	275-277	3
α-helix	283-300	18
β-strand	305-308	4	1
α-helix	320-337	18
β-strand	345-350	6	1
α-helix	353-364	12

Chain B: 6 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	184-190	7	2
β-strand	196-201	6	2
β-strand	211-215	5	2
α-helix	224-249	26
β-strand	257-261	5	2
β-strand	269-273	5	2
α-helix	275-277	3
α-helix	283-300	18
β-strand	305-309	5	2
β-strand	313	1	3
α-helix	314-316	3
β-strand	318	1	3
α-helix	320-337	18
β-strand	345-349	5	2
α-helix	353-363	11

Chain C: 5 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	184-190	7	4
β-strand	196-201	6	4
β-strand	211-216	6	4
α-helix	224-249	26
β-strand	257-261	5	4
β-strand	269-274	6	4
α-helix	275-277	3
α-helix	283-300	18
β-strand	305-308	4	4
β-strand	313	1	5
β-strand	318	1	5
α-helix	320-337	18
β-strand	345-350	6	4
α-helix	353-365	13

Chain D: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	184-190	7	6
β-strand	196-201	6	6
α-helix	204-206	3
β-strand	211-216	6	6
α-helix	225-249	25
β-strand	257-261	5	6
β-strand	269-274	6	6
α-helix	275-277	3
α-helix	283-300	18
β-strand	305-308	4	6
β-strand	313	1	7
α-helix	314-316	3
β-strand	318	1	7
α-helix	320-337	18
β-strand	345-349	5	6
α-helix	353-365	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
histone macroH2A1.1	A, B, C, D	protein	211	Homo sapiens	O75367 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>1ZR3_1 histone macroH2A1.1 (chains A, B, C, D)
GAMQGEVSKAASADSTTEGTPADGFTVLSTKSLFLGQKLQVVQADIASIDSDAVVHPTNT
DFYIGGEVGNTLEKKGGKEFVEAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSPVW
GADKCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVST
MSSSIKTVYFVLFDSESIGIYVQEMAKLDAN

Primary citation

Splicing regulates NAD metabolite binding to histone macroH2A. Kustatscher, G., Hothorn, M., Pugieux, C. et al. Nat Struct Mol Biol (2005) 12:624-625. DOI 10.1038/nsmb956 · PubMed

Other PDB entries of the same protein (UniProt O75367 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3HSV 1.43 Å, Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of…
3IVB 1.75 Å, Structures of SPOP-Substrate Complexes: Insights into Architectures of BTB-Cul3…
3IID 1.9 Å, Crystal structure of the macro domain of human histone macroH2A1.1 in complex with…
3IIF 2.1 Å, Crystal structure of the macro domain of human histone macroH2A1.1 in complex with…
5IIT 2.13 Å, Structure of SPX domain of the yeast inorganic polyphophate polymerase Vtc4 crystallized…
3HQH 2.3 Å, Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of…
2FXK 2.54 Å, Crystal structure of the macro-domain of human core histone variant macroH2A1.1 (form A)
2F8N 2.9 Å, 2.9 Angstrom X-ray structure of hybrid macroH2A nucleosomes
9PM0 2.9 Å, nucleosome containing histone variant macroH2A
1ZR5 2.92 Å, Crystal structure of the macro-domain of human core histone variant macroH2A1.2
1U35 3.0 Å, Crystal structure of the nucleosome core particle containing the histone domain of…
7D3Y 3.11 Å, Crystal structure of the osPHR2-osSPX2 complex

Browse structure collections

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