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Crystal structures of the arginine-, lysine-, histidine-binding protein artj from the thermophilic bacterium geobacillus stearothermophilus
Analyse Crystal structures of the arginine-, lysine-, histidine-binding protein artj… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PVU
- Type
- protein
- Length
- 235 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Artj
- Ligands
- LYS, SO4
- Pockets
- 5 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Artj | protein | 235 | 39% helix, 24% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 92 | 0.46 | 0.80 | 20 | SO4 |
| 2 | 83 | 0.40 | 0.77 | 14 | empty |
| 3 | 74 | 0.34 | 0.76 | 16 | empty |
| 4 | 50 | 0.27 | 0.74 | 10 | empty |
| 5 | 59 | 0.26 | 0.73 | 14 | empty |
Compared structures
- 2PVU · Crystal structures of the arginine-, lysine-, histidine-binding protein ArtJ from the… · 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
- Elsewhere: RCSB PDB 2PVU · PDBe 2PVU
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