MolNFT v1 · #136252 · protein
Structure of the human POT1-TPP1 telomeric complex
5UN7: “Structure of the human POT1-TPP1 telomeric complex”. X-ray diffraction, 2 ligands (K, ZN). MolNFT v1 #136252 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5UN7
- Type
- protein
- Length
- 363 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9NUX5, Q96AP0
- Ligands
- K, ZN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 302 | — | Q9NUX5 |
| B | — | protein | 61 | — | Q96AP0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5UN7 · Structure of the human POT1-TPP1 telomeric complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q9NUX5 · AlphaFold monomer V2.0 prediction for protection of telomeres protein 1 (Q9NUX5) · a predicted model of the same protein · chain A against A, TM-score 0.96
- Q96AP0 · AlphaFold monomer V2.0 prediction for adrenocortical dysplasia protein homolog (Q96AP0) · a predicted model of the same protein · chain B against A, TM-score 0.30
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 Q9NUX5
- Every structure of UniProt Q96AP0
- Elsewhere: RCSB PDB 5UN7 · PDBe 5UN7 · UniProt Q9NUX5 · UniProt Q96AP0
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