MolNFT v1 · #155652 · protein + DNA
The human telomeric nucleosome displays distinct structural and dynamic properties
6LE9: “The human telomeric nucleosome displays distinct structural and dynamic properties”. X-ray diffraction, 1 ligand (MN). MolNFT v1 #155652 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6LE9
- Type
- protein + DNA
- Length
- 1,043 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P68431, P62805, P04908, O60814
- Ligands
- MN
Structure
x-ray diffraction · 10 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 95 | — | P68431 |
| B | — | protein | 87 | — | P62805 |
| C | — | protein | 103 | — | P04908 |
| D | — | protein | 95 | — | O60814 |
| E | — | protein | 96 | — | P68431 |
| F | — | protein | 78 | — | P62805 |
| G | — | protein | 105 | — | P04908 |
| H | — | protein | 94 | — | O60814 |
| I | — | dna | 145 | — | — |
| J | — | dna | 145 | — | — |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 4 copies · chains A, I, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6LE9 · The Human Telomeric Nucleosome Displays Distinct Structural and Dynamic Properties · the same entry in another collection · chain J against J, TM-score 1.00
- O60814 · AlphaFold monomer V2.0 prediction for histone H2B type 1-K (O60814) · a predicted model of the same protein · chain H against A, TM-score 0.88
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 P68431
- Every structure of UniProt P62805
- Every structure of UniProt P04908
- Every structure of UniProt O60814
- Elsewhere: RCSB PDB 6LE9 · PDBe 6LE9 · UniProt P68431 · UniProt P62805 · UniProt P04908 · UniProt O60814
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