Research workbench
Structure of a natural chimera of meningococcal factor H binding protein belonging to NL096 strain
Analyse Structure of a natural chimera of meningococcal factor H binding protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NRU
- Type
- protein
- Length
- 239 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Factor H binding protein variant 1-2,3.X
- UniProt
- C0JF81
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 62% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Factor H binding protein variant 1-2,3.X | protein | 239 | 6% helix, 62% strand | C0JF81 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 57 | 0.31 | 0.76 | 16 | empty |
Compared structures
- 7NRU · Structure of a natural chimera of meningococcal factor H binding protein belonging to… · 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 C0JF81
- Elsewhere: RCSB PDB 7NRU · PDBe 7NRU · UniProt C0JF81
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