Research workbench
Structure of the 4_601_157 tetranucleosome (P1 form)
Analyse Structure of the 4_601_157 tetranucleosome (P1 form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OY7
- Type
- protein + DNA
- Length
- 4,241 residues
- Chains
- 34
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone H2B 1.1; Histone H3; Histone H4; Histone H2A; DNA (619-mer)
- UniProt
- P02281, Q92133, P62799, Q6AZJ8
- Ligands
- CL
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 11 distinct chains · 63% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L, D, T, b | Histone H2B 1.1 | protein | 95 | 74% helix, 4% strand | P02281 |
| M, E, U, c | Histone H3 | protein | 97 | 65% helix, 4% strand | Q92133 |
| N, F, V, d | Histone H4 | protein | 78 | 65% helix, 8% strand | P62799 |
| O, G, W, e | Histone H2A | protein | 105 | 54% helix, 7% strand | Q6AZJ8 |
| P, H, X, f | Histone H2B 1.1 | protein | 93 | 75% helix, 4% strand | P02281 |
| Q, I, A, Y | Histone H3 | protein | 97 | 66% helix, 4% strand | Q92133 |
| R | Histone H4 | protein | 82 | 55% helix, 9% strand | P62799 |
| J, B, Z | Histone H4 | protein | 83 | 60% helix, 8% strand | P62799 |
| C, K, S, a | Histone H2A | protein | 103 | 56% helix, 6% strand | Q6AZJ8 |
| g | DNA (619-mer) | dna | 619 | — | — |
| h | DNA (619-mer) | dna | 619 | — | — |
Ligands and binding sites
- CL · Chloride ion · ion · 8 copies · chains O, P, g, C, D, h, G, H, L, K, S, T, W, X, a, b, e, f
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 768 | 0.79 | 0.83 | 76 | empty |
| 2 | 514 | 0.78 | 0.85 | 60 | empty |
| 3 | 487 | 0.77 | 0.85 | 56 | empty |
| 4 | 650 | 0.77 | 0.83 | 67 | empty |
| 5 | 618 | 0.77 | 0.83 | 66 | empty |
Interfaces
141 interfaces between chains.
- g–h · 28265 Ų buried · 2,948 hydrogen bonds · nucleic-nucleic
- a–b · 2695 Ų buried · 30 hydrogen bonds · protein-protein
- S–T · 2693 Ų buried · 30 hydrogen bonds · protein-protein
- L–K · 2692 Ų buried · 30 hydrogen bonds · protein-protein
- C–D · 2688 Ų buried · 30 hydrogen bonds · protein-protein
Compared structures
- 5OY7 · Structure of the 4_601_157 tetranucleosome (P1 form) · the same entry in another collection · chain L against L, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P02281
- Every structure of UniProt Q92133
- Every structure of UniProt P62799
- Every structure of UniProt Q6AZJ8
- Elsewhere: RCSB PDB 5OY7 · PDBe 5OY7 · UniProt P02281 · UniProt Q92133 · UniProt P62799 · UniProt Q6AZJ8
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