Research workbench
Structure treponema denticola factor H binding protein
Analyse Structure treponema denticola 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
- 3R15
- Type
- protein
- Length
- 156 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Factor H binding protein
- UniProt
- Q73RI0
- Ligands
- SCN
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Factor H binding protein | protein | 78 | 51% helix, 15% strand | Q73RI0 |
Ligands and binding sites
- SCN · Thiocyanate ion · ion · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 178 | 0.77 | 0.93 | 26 | empty |
| 2 | 66 | 0.32 | 0.75 | 14 | empty |
| 3 | 61 | 0.30 | 0.74 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 533 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3R15 · Structure Treponema Denticola Factor H Binding Protein · 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 Q73RI0
- Elsewhere: RCSB PDB 3R15 · PDBe 3R15 · UniProt Q73RI0
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