Research workbench
Complement regulator acquiring outer surface protein bbcrasp-4 or erpc from borrelia burgdorferi
Analyse Complement regulator acquiring outer surface protein bbcrasp-4 or erpc from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BOD
- Type
- protein
- Length
- 265 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Erpc
- UniProt
- Q44790
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Erpc | protein | 133 | 16% helix, 49% strand | Q44790 |
| B | Erpc | protein | 132 | 18% helix, 53% strand | Q44790 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 290 | 0.55 | 0.76 | 34 | empty |
| 2 | 185 | 0.47 | 0.75 | 22 | empty |
| 3 | 100 | 0.46 | 0.80 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 423 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 4BOD · Complement regulator acquiring outer surface protein BbCRASP-4 or ErpC from Borrelia… · 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 Q44790
- Elsewhere: RCSB PDB 4BOD · PDBe 4BOD · UniProt Q44790
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