Research workbench
Structure of the nicotinate-nucleotide pyrophosphorylase from francisella tularensis.
Analyse Structure of the nicotinate-nucleotide pyrophosphorylase from francisella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TQV
- Type
- protein
- Length
- 556 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nicotinate-nucleotide pyrophosphorylase
- EC
- 2.4.2.19
- UniProt
- Q5NEY8
- Ligands
- PO4
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nicotinate-nucleotide pyrophosphorylase (EC 2.4.2.19) | protein | 276 | 41% helix, 20% strand | Q5NEY8 |
| B | Nicotinate-nucleotide pyrophosphorylase (EC 2.4.2.19) | protein | 280 | 42% helix, 20% strand | Q5NEY8 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 415 | 0.72 | 0.83 | 44 | PO4 |
| 2 | 418 | 0.71 | 0.83 | 43 | PO4 |
| 3 | 303 | 0.55 | 0.75 | 38 | empty |
| 4 | 84 | 0.51 | 0.83 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 2674 Ų buried · 34 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 3TQV · Structure of the nicotinate-nucleotide pyrophosphorylase from Francisella tularensis. · 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 Q5NEY8
- Elsewhere: RCSB PDB 3TQV · PDBe 3TQV · UniProt Q5NEY8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.