Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Determined by X-ray diffraction at 2.35 Å resolution. Released 29 May 2013.
Explore 4KHA in 3D Show helices and sheets RCSB PDB PDBe
4KHA contains 25 α-helices and 23 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 |
|---|---|---|---|
| α-helix | 654-659 | 6 | |
| α-helix | 663-665 | 3 | |
| β-strand | 666-670 | 5 | 1 |
| β-strand | 671-673 | 3 | 2 |
| β-strand | 683-687 | 5 | 1 |
| β-strand | 691-695 | 5 | 1 |
| β-strand | 703-707 | 5 | 1 |
| α-helix | 708-710 | 3 | |
| β-strand | 711-717 | 7 | 2 |
| β-strand | 724-737 | 14 | 2 |
| β-strand | 740-750 | 11 | 2 |
| α-helix | 783-804 | 22 | |
| α-helix | 806-808 | 3 | |
| β-strand | 812-813 | 2 | 2 |
| α-helix | 817-819 | 3 | |
| β-strand | 821-823 | 3 | 3 |
| β-strand | 824 | 1 | 4 |
| β-strand | 830-832 | 3 | 3 |
| β-strand | 833-834 | 2 | 5 |
| β-strand | 838-841 | 4 | 5 |
| α-helix | 847 | 1 | |
| β-strand | 848-851 | 4 | 5 |
| α-helix | 852-854 | 3 | |
| β-strand | 855-861 | 7 | 6 |
| β-strand | 869-876 | 8 | 6 |
| α-helix | 882-883 | 2 | |
| β-strand | 884-890 | 7 | 6 |
| α-helix | 891-893 | 3 | |
| α-helix | 894-903 | 10 | |
| β-strand | 908-910 | 3 | 6 |
| α-helix | 917-926 | 10 | |
| α-helix | 928-933 | 6 | |
| α-helix | 936-940 | 5 | |
| α-helix | 1031-1033 | 3 | |
| α-helix | 1035-1045 | 11 | |
| β-strand | 1050-1051 | 2 | 7 |
| α-helix | 1053-1080 | 28 | |
| β-strand | 1085-1086 | 2 | 8 |
| α-helix | 1088-1098 | 11 | |
| α-helix | 1101-1120 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-16 | 3 | |
| α-helix | 17-21 | 5 | |
| α-helix | 27-36 | 10 | |
| β-strand | 42-43 | 2 | 8 |
| α-helix | 46-72 | 27 | |
| β-strand | 77-78 | 2 | 7 |
| α-helix | 80-88 | 9 | |
| α-helix | 91-97 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Spt16M-Histone H2B 1.1 chimera | A | protein | 410 | Chaetomium thermophilum var. thermophilum, Xenopus laevis | G0SDN1 (AlphaFold model), P02281 (AlphaFold model) |
| Histone H2A | B | protein | 92 | Xenopus laevis | Q6AZJ8 (AlphaFold model) |
>4KHA_1 Spt16M-Histone H2B 1.1 chimera (chains A) GHMDVVEQDKLIEIRNRRPAVLDNVYIRPALEGKRVPGKVEIHQNGIRYQSPLSTTQRVD VLFSNIRHLFFQPCQNEMIVIIHLHLKDPILFGKKKTKDVQFYREAIDIQFDETGNRKRK YRYGDEDEFEAEQEERRRKAELDRLFKSFAEKIAEAGRNEGIEVDMPIRDLGFNGVPNRS NVVIYPTTECLIQITEPPFLVITLEDVEWAHLERVQFGLKNFDLVFVFKDFTRPVVHINT IPVESLEDVKEFLDSSDIPFSEGPLNLNWSVIMKTVTANPHQFFLDGGWGFLQNDSDGSG GSGGSGGSGGSKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAG EASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK
>4KHA_2 Histone H2A (chains B) AGRAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAA RDNKKTRIIPRHLQLAVRNDEELNKLLGRVTI
Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Hondele, M., Stuwe, T., Hassler, M. et al. Nature (2013) 499:111-114. DOI 10.1038/nature12242 · PubMed
Other PDB entries of the same protein (UniProt G0SDN1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4KHA directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.