Research workbench
Bbcrasp-1 from borrelia burgdorferi
Analyse Bbcrasp-1 from borrelia burgdorferi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1W33
- Type
- protein
- Length
- 361 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bbcrasp-1
- UniProt
- Q7AUV9
- Pockets
- 2 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bbcrasp-1 | protein | 181 | 81% helix, 0% strand | Q7AUV9 |
| B | Bbcrasp-1 | protein | 180 | 79% helix, 0% strand | Q7AUV9 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
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 | 158 | 0.49 | 0.77 | 21 | GOL |
| 2 | 85 | 0.40 | 0.78 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 2366 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 1W33 · BbCRASP-1 from Borrelia Burgdorferi · 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 Q7AUV9
- Elsewhere: RCSB PDB 1W33 · PDBe 1W33 · UniProt Q7AUV9
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