4XZQ: Histone H3.2
Nucleosome disassembly by RSC and SWI/SNF is enhanced by H3 acetylation near the nucleosome dyad axis. Determined by X-ray diffraction at 2.4 Å resolution. Released 14 Oct 2015.
- Method
- X-ray diffraction
- Resolution
- 2.4 Å
- Organisms
- Xenopus laevis, Homo sapiens
- Chains
- 10
- Atoms
- 12,090
- Mol. weight
- 175.84 kDa
- Released
- 14 Oct 2015
Explore 4XZQ in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4XZQ contains 38 α-helices and 20 β-strands across 8 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 | 441-442 | 2 | |
| α-helix | 445-454 | 10 | |
| α-helix | 464-476 | 13 | |
| β-strand | 483-484 | 2 | 1 |
| α-helix | 486-513 | 28 | |
| β-strand | 518-519 | 2 | 2 |
| α-helix | 521-531 | 11 | |
Chain B: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-28 | 3 | |
| α-helix | 31-40 | 10 | |
| β-strand | 45-46 | 2 | 2 |
| α-helix | 50-75 | 26 | |
| β-strand | 80-81 | 2 | 1 |
| α-helix | 83-92 | 10 | |
| β-strand | 96-98 | 3 | 3 |
Chain C: 6 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 817-821 | 5 | |
| α-helix | 827-836 | 10 | |
| β-strand | 842-843 | 2 | 4 |
| α-helix | 846-872 | 27 | |
| β-strand | 877-878 | 2 | 5 |
| α-helix | 880-888 | 9 | |
| α-helix | 891-896 | 6 | |
| β-strand | 900-902 | 3 | 6 |
| α-helix | 913-915 | 3 | |
Chain D: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1235-1245 | 11 | |
| β-strand | 1250-1251 | 2 | 5 |
| α-helix | 1253-1280 | 28 | |
| β-strand | 1285-1286 | 2 | 4 |
| α-helix | 1288-1298 | 11 | |
| α-helix | 1301-1319 | 19 | |
Chain E: 5 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 641-642 | 2 | |
| α-helix | 645-656 | 12 | |
| α-helix | 664-676 | 13 | |
| β-strand | 683-684 | 2 | 7 |
| α-helix | 686-713 | 28 | |
| β-strand | 718-719 | 2 | 8 |
| α-helix | 721-731 | 11 | |
Chain F: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 225-228 | 4 | |
| α-helix | 231-240 | 10 | |
| β-strand | 245-246 | 2 | 8 |
| α-helix | 250-275 | 26 | |
| β-strand | 280-281 | 2 | 7 |
| α-helix | 283-292 | 10 | |
| β-strand | 296-298 | 3 | 6 |
Chain G: 6 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1017-1020 | 4 | |
| α-helix | 1027-1036 | 10 | |
| β-strand | 1042-1043 | 2 | 9 |
| α-helix | 1047-1071 | 25 | |
| β-strand | 1077-1078 | 2 | 10 |
| α-helix | 1080-1088 | 9 | |
| α-helix | 1091-1096 | 6 | |
| β-strand | 1100-1102 | 3 | 3 |
| α-helix | 1113-1115 | 3 | |
Chain H: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1435-1445 | 11 | |
| β-strand | 1450-1451 | 2 | 10 |
| α-helix | 1453-1480 | 28 | |
| β-strand | 1485-1486 | 2 | 9 |
| α-helix | 1488-1498 | 11 | |
| α-helix | 1501-1519 | 19 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Histone H3.2 | A, E | protein | 98 | Xenopus laevis | P84233 (AlphaFold model) |
| Histone H4 | B, F | protein | 79 | Xenopus laevis | P62799 (AlphaFold model) |
| Histone H2A | C, G | protein | 107 | Xenopus laevis | P06897 (AlphaFold model) |
| Histone H2B 1.1 | D, H | protein | 93 | Xenopus laevis | P02281 (AlphaFold model) |
| DNA (147-mer) | I | DNA | 147 | Homo sapiens | |
| DNA (147-mer) | J | DNA | 147 | Homo sapiens | |
Sequence of entity 1 (A, E), FASTA
>4XZQ_1 Histone H3.2 (chains A, E)
PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASE
AYLVALFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
Sequence of entity 2 (B, F), FASTA
>4XZQ_2 Histone H4 (chains B, F)
DNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTA
MDVVYALKRQGRTLYGFGG
Sequence of entity 3 (C, G), FASTA
>4XZQ_3 Histone H2A (chains C, G)
AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDN
KKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKT
Sequence of entity 4 (D, H), FASTA
>4XZQ_4 Histone H2B 1.1 (chains D, H)
RKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHYNKRSTITSR
EIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK
Sequence of entity 5 (I), FASTA
>4XZQ_5 DNA (147-MER) (chains I)
ATCAATATCCACCTGCAGATACTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGC
ATGTTCAGCTGGAATCCAGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTT
TGGTAGTATCTGCAGGTGGATATTGAT
Sequence of entity 6 (J), FASTA
>4XZQ_6 DNA (147-MER) (chains J)
ATCAATATCCACCTGCAGATACTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGC
ATGTTCAGCTGGATTCCAGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTT
TGGTAGTATCTGCAGGTGGATATTGAT
Primary citation
Histone Acetylation near the Nucleosome Dyad Axis Enhances Nucleosome Disassembly by RSC and SWI/SNF. Chatterjee, N., North, J.A., Dechassa, M.L. et al. Mol Cell Biol (2015) 35:4083-4092. DOI 10.1128/MCB.00441-15 · PubMed
Other PDB entries of the same protein (UniProt P84233 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2HUE 1.7 Å, Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4
- 3GV6 1.76 Å, Crystal Structure of human chromobox homolog 6 (CBX6) with H3K9 peptide
- 1KX5 1.94 Å, X-Ray Structure of the Nucleosome Core Particle, NCP147, at 1.9 A Resolution
- 1KX3 2.0 Å, X-Ray Structure of the Nucleosome Core Particle, NCP146, at 2.0 A Resolution
- 4QEO 2.0 Å, crystal structure of KRYPTONITE in complex with mCHH DNA, H3(1-15) peptide and SAH
- 1S32 2.05 Å, Molecular Recognition of the Nucleosomal 'Supergroove'
- 3UTA 2.07 Å, Crystal Structure of Nucleosome Core Particle Assembled with an Alpha-Satellite Sequence…
- 3C1B 2.2 Å, The effect of H3 K79 dimethylation and H4 K20 trimethylation on nucleosome and chromatin…
- 3UT9 2.2 Å, Crystal Structure of Nucleosome Core Particle Assembled with a Palindromic Widom '601'…
- 3UTB 2.2 Å, Crystal Structure of Nucleosome Core Particle Assembled with the 146b Alpha-Satellite…
- 6WZ5 2.2 Å, Bridging of double-strand DNA break activates PARP2/HPF1 to modify chromatin
- 8RUQ 2.29 Å, Borealin N-terminus in complex with H3.T3p-nucleosome
Browse structure collections
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