Research workbench
The crystal structure of the inorganic triphosphatase NE1496
Analyse The crystal structure of the inorganic triphosphatase NE1496 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TYP
- Type
- protein
- Length
- 296 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- Q82UI9
- Ligands
- NA
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 146 | 20% helix, 44% strand | Q82UI9 |
| B | Uncharacterized protein | protein | 150 | 18% helix, 43% strand | Q82UI9 |
Ligands and binding sites
- NA · Sodium ion · metal · 8 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
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 | 82 | 0.42 | 0.79 | 17 | empty |
| 2 | 83 | 0.37 | 0.76 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 807 Ų buried · 10 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 Q82UI9
- Elsewhere: RCSB PDB 3TYP · PDBe 3TYP · UniProt Q82UI9
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