Research workbench
Insights to complement factor H recruitment by the borrelial cspz protein as revealed by structural analysis
Analyse Insights to complement factor H recruitment by the borrelial cspz protein as… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ATG
- Type
- protein
- Length
- 543 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HCG40889, isoform CRA_B; Complement regulator-acquiring surface protein 2 (crasp-2)
- UniProt
- A0A024R962, O50665
- Ligands
- MG
- Pockets
- 5 · best druggability 0.58
Structure
x-ray diffraction · 4 distinct chains · 61% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HCG40889, isoform CRA_B | protein | 59 | 5% helix, 36% strand | A0A024R962 |
| B | Complement regulator-acquiring surface protein 2 (crasp-2) | protein | 212 | 80% helix, 0% strand | O50665 |
| C | Complement regulator-acquiring surface protein 2 (crasp-2) | protein | 211 | 75% helix, 0% strand | O50665 |
| D | HCG40889, isoform CRA_B | protein | 61 | 5% helix, 34% strand | A0A024R962 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 318 | 0.58 | 0.77 | 41 | empty |
| 2 | 188 | 0.49 | 0.76 | 28 | empty |
| 3 | 59 | 0.39 | 0.80 | 18 | empty |
| 4 | 88 | 0.36 | 0.75 | 17 | empty |
| 5 | 66 | 0.28 | 0.73 | 18 | empty |
Interfaces
4 interfaces between chains.
- A–B · 898 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 866 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 406 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 45 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6ATG · Insights to complement factor H recruitment by the borrelial CspZ protein as revealed by… · 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 A0A024R962
- Every structure of UniProt O50665
- Elsewhere: RCSB PDB 6ATG · PDBe 6ATG · UniProt A0A024R962 · UniProt O50665
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