Research workbench
Crystal structure of a telomere single-strand DNA-protein complex from O. nova with full-length alpha and beta telomere proteins
Analyse Crystal structure of a telomere single-strand DNA-protein complex from O. nova… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2I0Q
- Type
- protein + DNA
- Length
- 688 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P29549, P16458
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | — | dna | 11 | — | — |
| A | — | protein | 461 | — | P29549 |
| B | — | protein | 216 | — | P16458 |
Compared structures
- 2I0Q · Crystal structure of a telomere single-strand DNA-protein complex from O. nova with… · the same entry in another collection · chain D against D, TM-score 1.00
- P16458 · AlphaFold monomer V2.0 prediction for telomere-binding protein subunit beta (P16458) · a predicted model of the same protein · chain B against A, TM-score 0.99
- P29549 · AlphaFold monomer V2.0 prediction for telomere-binding protein subunit alpha (P29549) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P29549
- Every structure of UniProt P16458
- Elsewhere: RCSB PDB 2I0Q · PDBe 2I0Q · UniProt P29549 · UniProt P16458
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