Crystal structure of human SPT16 Mid-AID/H3-H4 tetramer FACT Histone complex. Determined by X-ray diffraction at 2.98 Å resolution. Released 9 Mar 2016.
Explore 4Z2M in 3D Show helices and sheets RCSB PDB PDBe
4Z2M contains 22 α-helices and 27 β-strands across 5 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 | 661-668 | 8 | 1 |
| β-strand | 677-682 | 6 | 1 |
| β-strand | 686-691 | 6 | 1 |
| β-strand | 696-700 | 5 | 1 |
| β-strand | 704-710 | 7 | 1 |
| β-strand | 717-729 | 13 | 1 |
| β-strand | 734-743 | 10 | 1 |
| β-strand | 747-749 | 3 | 2 |
| α-helix | 764-790 | 27 | |
| β-strand | 797-798 | 2 | 1 |
| α-helix | 799-800 | 2 | |
| α-helix | 802-804 | 3 | |
| β-strand | 806-808 | 3 | 3 |
| β-strand | 809 | 1 | 4 |
| β-strand | 815-817 | 3 | 3 |
| β-strand | 818-819 | 2 | 5 |
| β-strand | 823-826 | 4 | 5 |
| β-strand | 833-836 | 4 | 5 |
| α-helix | 837-839 | 3 | |
| β-strand | 840-846 | 7 | 6 |
| β-strand | 854-861 | 8 | 6 |
| α-helix | 867-868 | 2 | |
| β-strand | 869-875 | 7 | 6 |
| α-helix | 876-878 | 3 | |
| α-helix | 879-888 | 10 | |
| β-strand | 893-896 | 4 | 6 |
| α-helix | 902-910 | 9 | |
| α-helix | 915-918 | 4 | |
| α-helix | 921-925 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 64-73 | 10 | |
| β-strand | 83-84 | 2 | 7 |
| α-helix | 86-113 | 28 | |
| β-strand | 118-119 | 2 | 2 |
| α-helix | 121-131 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 31-41 | 11 | |
| β-strand | 45-47 | 3 | 2 |
| α-helix | 50-75 | 26 | |
| β-strand | 80-81 | 2 | 7 |
| α-helix | 83-92 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 64-75 | 12 | |
| β-strand | 83-84 | 2 | 8 |
| α-helix | 86-113 | 28 | |
| β-strand | 118-119 | 2 | 9 |
| α-helix | 121-131 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 31-40 | 10 | |
| β-strand | 45-46 | 2 | 9 |
| α-helix | 50-73 | 24 | |
| β-strand | 80-81 | 2 | 8 |
| α-helix | 83-90 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| FACT complex subunit SPT16 | B | protein | 287 | Homo sapiens | Q9Y5B9 (AlphaFold model) |
| Histone H3.1 | G, I | protein | 102 | Homo sapiens | P68431 (AlphaFold model) |
| Histone H4 | H, J | protein | 103 | Homo sapiens | P62805 (AlphaFold model) |
>4Z2M_1 FACT complex subunit SPT16 (chains B) GIVKQDSLVINLNRSNPKLKDLYIRPNIAQKRMQGSLEAHVNGFRFTSVRGDKVDILYNN IKHALFQPCDGEMIIVLHFHLKNAIMFGKKRHTDVQFYTEVGEITTDLGKHQHMHDRDDL YAEQMEREMRHKLKTAFKNFIEKVEALTKEELEFEVPFRDLGFNGAPYRSTCLLQPTSSA LVNATEWPPFVVTLDEVELIHFERVQFHLKNFDMVIVYKDYSKKVTMINAIPVASLDPIK EWLNSCDLKYTEGVQSLNWTKIMKTIVDDPEGFFEQGGWSFLEPEGE
>4Z2M_2 Histone H3.1 (chains G, I) GVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQ EACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
>4Z2M_3 Histone H4 (chains H, J) MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLK VFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Integrated molecular mechanism directing nucleosome reorganization by human FACT. Tsunaka, Y., Fujiwara, Y., Oyama, T. et al. Genes Dev (2016) 30:673-686. DOI 10.1101/gad.274183.115 · PubMed
Other PDB entries of the same protein (UniProt Q9Y5B9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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