MolNFT v1 · #12507 · protein + DNA
Dimeric structure of the O. nova telomere end binding protein alpha subunit with bound ssdna
1KIX · 5'-D(*T*TP*TP*TP*GP*GP*GP*G)-3': “Dimeric structure of the O. nova telomere end binding protein alpha subunit with bound ssdna”. X-ray diffraction, 1 ligand (SO4), 4 pockets (best druggability 0.72). MolNFT v1 #12507 on GenesisL1…
- 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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