Research workbench
Crystal structure of inorganic pyrophosphatase from Ehrlichia chaffeensis
Analyse Crystal structure of inorganic pyrophosphatase from Ehrlichia chaffeensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LO0
- Type
- protein
- Length
- 156 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.95
- Source
- Ehrlichia chaffeensis
- Molecule
- Inorganic pyrophosphatase
- EC
- 3.6.1.1
- UniProt
- Q2GFI3
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · resolution 1.95 · 1 distinct chain · 19% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inorganic pyrophosphatase (EC 3.6.1.1) | protein | 156 | 19% helix, 37% strand | Q2GFI3 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 155 | 0.44 | 0.75 | 32 | SO4 |
Compared structures
- 3LO0 · Crystal structure of inorganic pyrophosphatase from ehrlichia chaffeensis · 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 Q2GFI3
- Elsewhere: RCSB PDB 3LO0 · PDBe 3LO0 · UniProt Q2GFI3
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