Research workbench
Dimeric structure of the O. nova telomere end binding protein alpha subunit with bound ssdna
Analyse Dimeric structure of the O. nova telomere end binding protein alpha subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KIX
- Type
- protein + DNA
- Length
- 453 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-D(*T*TP*TP*TP*GP*GP*GP*G)-3'; Telomere-binding protein alpha subunit
- UniProt
- P29549
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | 5'-D(*T*TP*TP*TP*GP*GP*GP*G)-3' | dna | 7 | — | — |
| A | Telomere-binding protein alpha subunit | protein | 446 | 17% helix, 37% strand | P29549 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 745 | 0.72 | 0.78 | 71 | empty |
| 2 | 77 | 0.36 | 0.77 | 22 | empty |
| 3 | 52 | 0.32 | 0.77 | 11 | empty |
| 4 | 55 | 0.31 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- D–A · 916 Ų buried · 35 hydrogen bonds · protein-nucleic
Compared structures
- 1KIX · Dimeric Structure of the O. nova Telomere End Binding Protein Alpha Subunit with Bound… · the same entry in another collection · chain A against A, TM-score 1.00
- 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 0.60
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
- Elsewhere: RCSB PDB 1KIX · PDBe 1KIX · UniProt P29549
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