Crystal structure of the macro-domain of human core histone variant macroH2A1.2. Determined by X-ray diffraction at 2.92 Å resolution. Released 21 Jun 2005.
Explore 1ZR5 in 3D Show helices and sheets RCSB PDB PDBe
1ZR5 contains 13 α-helices and 14 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 182-188 | 7 | 1 |
| β-strand | 194-199 | 6 | 1 |
| α-helix | 202-207 | 6 | |
| β-strand | 212-216 | 5 | 1 |
| α-helix | 226-250 | 25 | |
| β-strand | 258-262 | 5 | 1 |
| β-strand | 270-274 | 5 | 1 |
| α-helix | 276-278 | 3 | |
| α-helix | 284-301 | 18 | |
| β-strand | 306-309 | 4 | 1 |
| α-helix | 321-338 | 18 | |
| β-strand | 346-351 | 6 | 1 |
| α-helix | 354-365 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 182-188 | 7 | 2 |
| β-strand | 194-199 | 6 | 2 |
| α-helix | 202-207 | 6 | |
| β-strand | 212-217 | 6 | 2 |
| α-helix | 226-233 | 8 | |
| α-helix | 236-250 | 15 | |
| β-strand | 258-262 | 5 | 2 |
| β-strand | 270-275 | 6 | 2 |
| α-helix | 276-278 | 3 | |
| α-helix | 284-301 | 18 | |
| β-strand | 306-309 | 4 | 2 |
| α-helix | 321-338 | 18 | |
| β-strand | 346-351 | 6 | 2 |
| α-helix | 354-365 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| H2AFY protein | A, B | protein | 214 | Homo sapiens | O75367 (AlphaFold model) |
>1ZR5_1 H2AFY protein (chains A, B) GAKQGEVSKAASADSTTEGTPADGFTVLSTKSLFLGQKLNLIHSEISNLAGFEVEAIINP TNADIDLKDDLGNTLEKKGGKEFVEAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNS PVWGADKCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYF VSTMSSSIKTVYFVLFDSESIGIYVQEMAKLDAN
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:
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