Research workbench
Neutral trehalase NTH1 from saccharomyces cerevisiae
Analyse Neutral trehalase NTH1 from saccharomyces cerevisiae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NIS
- Type
- protein
- Length
- 550 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neutral trehalase
- EC
- 3.2.1.28
- UniProt
- P32356
- Pockets
- 8 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neutral trehalase (EC 3.2.1.28) | protein | 550 | 52% helix, 9% strand | P32356 |
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 331 | 0.63 | 0.79 | 27 | empty |
| 2 | 179 | 0.49 | 0.77 | 23 | empty |
| 3 | 131 | 0.46 | 0.77 | 24 | empty |
| 4 | 126 | 0.39 | 0.74 | 18 | empty |
| 5 | 101 | 0.37 | 0.75 | 27 | empty |
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 P32356
- Elsewhere: RCSB PDB 5NIS · PDBe 5NIS · UniProt P32356
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