3C1C: Histone H3-like
The effect of H3 K79 dimethylation and H4 K20 trimethylation on nucleosome and chromatin structure. Determined by X-ray diffraction at 3.15 Å resolution. Released 7 Oct 2008.
- Method
- X-ray diffraction
- Resolution
- 3.15 Å
- Organisms
- Xenopus laevis, Xenopus (Silurana) tropicalis
- Chains
- 10
- Atoms
- 12,230
- Mol. weight
- 198.9 kDa
- Released
- 7 Oct 2008
Explore 3C1C in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3C1C contains 39 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 | 445-456 | 12 | |
| α-helix | 464-475 | 12 | |
| β-strand | 483-484 | 2 | 1 |
| α-helix | 486-513 | 28 | |
| β-strand | 518-519 | 2 | 2 |
| α-helix | 521-530 | 10 | |
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 | 97-98 | 2 | 3 |
Chain C: 6 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 817-821 | 5 | |
| α-helix | 827-835 | 9 | |
| 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 | 901-902 | 2 | 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 | 645-654 | 10 | |
| α-helix | 664-678 | 15 | |
| 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 | 225-227 | 3 | |
| 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 | 297-298 | 2 | 6 |
Chain G: 7 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1017-1020 | 4 | |
| α-helix | 1027-1035 | 9 | |
| β-strand | 1042-1043 | 2 | 9 |
| α-helix | 1046-1071 | 26 | |
| β-strand | 1077-1078 | 2 | 10 |
| α-helix | 1080-1087 | 8 | |
| α-helix | 1091-1096 | 6 | |
| β-strand | 1101-1102 | 2 | 3 |
| α-helix | 1113-1115 | 3 | |
| α-helix | 1117-1118 | 2 | |
Chain H: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1435-1443 | 9 | |
| 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-like | A, E | protein | 135 | Xenopus laevis | P84233 (AlphaFold model) |
| Histone H4 | B, F | protein | 102 | Xenopus laevis | P62799 (AlphaFold model) |
| Histone H2A type 1 | C, G | protein | 129 | Xenopus laevis | P06897 (AlphaFold model) |
| Histone 2, H2bf | D, H | protein | 125 | Xenopus (Silurana) tropicalis | Q28D68 (AlphaFold model) |
| Palindromic 146bp Human Alpha satellite DNA | I, J | DNA | 146 | | |
Sequence of entity 1 (A, E), FASTA
>3C1C_1 Histone H3-like (chains A, E)
ARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTEL
LIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLAAIHAKRVTIM
PKDIQLARRIRGERA
Sequence of entity 2 (B, F), FASTA
>3C1C_2 Histone H4 (chains B, F)
SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV
FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Sequence of entity 3 (C, G), FASTA
>3C1C_3 Histone H2A type 1 (chains C, G)
SGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTA
EILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKT
ESSKSTKSK
Sequence of entity 4 (D, H), FASTA
>3C1C_4 Histone 2, H2bf (chains D, H)
PDPAKSAPAAKKGSKKAVTKTQKKDGKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMS
IMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTK
YTSAK
Sequence of entity 5 (I, J), FASTA
>3C1C_5 Palindromic 146bp Human Alpha satellite DNA (chains I, J)
ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGC
ATGTTCAGCGGAATTCCGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTT
GGTAGAATCTGCAGGTGGATATTGAT
Primary citation
The effect of H3K79 dimethylation and H4K20 trimethylation on nucleosome and chromatin structure. Lu, X., Simon, M.D., Chodaparambil, J.V. et al. Nat Struct Mol Biol (2008) 15:1122-1124. DOI 10.1038/nsmb.1489 · 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
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