Research workbench
Crystal structure of the 14-3-3:NEUTRAL trehalase NTH1 complex
Analyse Crystal structure of the 14-3-3:NEUTRAL trehalase NTH1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5N6N
- Type
- protein
- Length
- 1,153 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein BMH1; Neutral trehalase
- EC
- 3.2.1.28
- UniProt
- P29311, P32356
- Ligands
- GLC, FRU, CA
- Pockets
- 13 · best druggability 0.86
Structure
x-ray diffraction · 3 distinct chains · 61% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein BMH1 | protein | 231 | 85% helix, 0% strand | P29311 |
| B | Protein BMH1 | protein | 224 | 83% helix, 0% strand | P29311 |
| C | Neutral trehalase (EC 3.2.1.28) | protein | 698 | 45% helix, 11% strand | P32356 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 3 copies · chains C
- FRU · beta-D-fructofuranose · sugar · 3 copies · chains C
- CA · Calcium ion · metal · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1107 | 0.86 | 0.87 | 106 | empty |
| 2 | 719 | 0.74 | 0.80 | 62 | GLC, FRU |
| 3 | 59 | 0.71 | 0.98 | 19 | empty |
| 4 | 452 | 0.67 | 0.79 | 87 | empty |
| 5 | 155 | 0.64 | 0.85 | 29 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1830 Ų buried · 31 hydrogen bonds · protein-protein
- B–C · 1386 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 1113 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 modified (artifact, phosphorylation).
Compared structures
- 5N6N · Crystal structure of the 14-3-3:NEUTRAL trehalase NTH1 complex · the same entry in another collection · chain A against A, TM-score 1.00
- P29311 · AlphaFold monomer V2.0 prediction for protein BMH1 (P29311) · a predicted model of the same protein · chain B against A, TM-score 0.99
- P32356 · AlphaFold monomer V2.0 prediction for neutral trehalase (P32356) · a predicted model of the same protein · chain C against A, TM-score 0.94
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 P29311
- Every structure of UniProt P32356
- Elsewhere: RCSB PDB 5N6N · PDBe 5N6N · UniProt P29311 · UniProt P32356
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