Research workbench
Crystal structure of bs-tpnppase
Analyse Crystal structure of bs-tpnppase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KN8
- Type
- protein
- Length
- 499 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thermostable nppase
- UniProt
- Q8L1N9
- Pockets
- 4 · best druggability 0.60
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, 20% strand | Q8L1N9 |
| B | Thermostable nppase | protein | 244 | 39% helix, 21% 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 | 343 | 0.60 | 0.77 | 47 | empty |
| 2 | 271 | 0.53 | 0.75 | 35 | empty |
| 3 | 92 | 0.39 | 0.76 | 24 | empty |
| 4 | 62 | 0.28 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1232 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 4KN8 · Crystal structure of Bs-TpNPPase · 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 4KN8 · PDBe 4KN8 · UniProt Q8L1N9
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