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Crystal structure of double mutant thermostable nppase from geobacillus stearothermophilus
Analyse Crystal structure of double mutant thermostable nppase from geobacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IFT
- Type
- protein
- Length
- 502 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thermostable nppase
- UniProt
- Q8L1N9
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thermostable nppase | protein | 255 | 42% helix, 19% strand | Q8L1N9 |
| B | Thermostable nppase | protein | 247 | 40% helix, 22% strand | Q8L1N9 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 382 | 0.63 | 0.78 | 54 | empty |
| 2 | 254 | 0.56 | 0.77 | 30 | empty |
| 3 | 62 | 0.33 | 0.76 | 15 | empty |
| 4 | 57 | 0.30 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1235 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 4IFT · Crystal structure of double mutant thermostable NPPase from Geobacillus stearothermophilus · 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 Q8L1N9
- Elsewhere: RCSB PDB 4IFT · PDBe 4IFT · UniProt Q8L1N9
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