Research workbench
Crystal structure of the first DH/PH domain of trio to 1.7 a
Analyse Crystal structure of the first DH/PH domain of trio to 1.7 a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NTY
- Type
- protein
- Length
- 305 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triple functional domain protein
- UniProt
- O75962
- Pockets
- 3 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triple functional domain protein | protein | 305 | 53% helix, 18% strand | O75962 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 66 | 0.38 | 0.79 | 20 | empty |
| 2 | 66 | 0.34 | 0.76 | 13 | empty |
| 3 | 50 | 0.26 | 0.74 | 13 | empty |
Compared structures
- 1NTY · Crystal structure of the first DH/PH domain of Trio to 1.7 A · the same entry in another collection · chain A against A, TM-score 1.00
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 O75962
- Elsewhere: RCSB PDB 1NTY · PDBe 1NTY · UniProt O75962
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