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Crystal structure of tetrahymena P45C
Analyse Crystal structure of tetrahymena P45C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DOK
- Type
- protein
- Length
- 339 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Telomerase associated protein P45
- UniProt
- Q6JXI5
- Ligands
- MG
- Pockets
- 6 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 59% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Telomerase associated protein P45 | protein | 170 | 58% helix, 9% strand | Q6JXI5 |
| B | Telomerase associated protein P45 | protein | 169 | 60% helix, 9% strand | Q6JXI5 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 288 | 0.54 | 0.76 | 32 | empty |
| 2 | 98 | 0.48 | 0.80 | 13 | empty |
| 3 | 60 | 0.44 | 0.83 | 14 | empty |
| 4 | 96 | 0.42 | 0.78 | 14 | empty |
| 5 | 61 | 0.39 | 0.79 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 549 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
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 Q6JXI5
- Elsewhere: RCSB PDB 5DOK · PDBe 5DOK · UniProt Q6JXI5
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