Research workbench
Dlp-2 from bacillus anthracis
Analyse Dlp-2 from bacillus anthracis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JIG
- Type
- protein
- Length
- 584 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dlp-2
- UniProt
- Q8RPQ1
- Ligands
- FE
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Dlp-2 | protein | 146 | 79% helix, 0% strand | Q8RPQ1 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 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 | 0.38 | 0.76 | 20 | empty |
| 2 | 85 | 0.32 | 0.73 | 18 | empty |
Interfaces
4 interfaces between chains.
- A–B · 1246 Ų buried · 19 hydrogen bonds · protein-protein
- C–D · 1245 Ų buried · 20 hydrogen bonds · protein-protein
- A–D · 410 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 379 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
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 Q8RPQ1
- Elsewhere: RCSB PDB 1JIG · PDBe 1JIG · UniProt Q8RPQ1
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