Research workbench
Structure of aspergillus fumigatus trehalose-6-phosphate phosphatase crystal form 2
Analyse Structure of aspergillus fumigatus trehalose-6-phosphate phosphatase crystal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DXN
- Type
- protein
- Length
- 265 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trehalose-6-phosphate phosphatase
- EC
- 2.4.1.15
- UniProt
- Q4WWF5
- Ligands
- MG
- Pockets
- 2 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trehalose-6-phosphate phosphatase (EC 2.4.1.15) | protein | 265 | 40% helix, 23% strand | Q4WWF5 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 205 | 0.49 | 0.75 | 34 | MG |
| 2 | 61 | 0.28 | 0.73 | 16 | empty |
Compared structures
- 5DXN · Structure of Aspergillus fumigatus trehalose-6-phosphate phosphatase crystal form 2 · 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 Q4WWF5
- Elsewhere: RCSB PDB 5DXN · PDBe 5DXN · UniProt Q4WWF5
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