MolNFT v1 · #64037 · protein
Crystal structure of flagellar protein flga from thermotoga maritima MSB8
3FRN: “Crystal structure of flagellar protein flga from thermotoga maritima MSB8”. X-ray diffraction, 1 pocket (best druggability 0.28). MolNFT v1 #64037 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3FRN
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar protein flga
- UniProt
- Q9X1M7
- Pockets
- 1 · best druggability 0.28
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flagellar protein flga | protein | 258 | 14% helix, 43% strand | Q9X1M7 |
Ligands and binding sites
- GOL · Glycerol · additive · 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 | 59 | 0.28 | 0.74 | 15 | empty |
Compared structures
- 3FRN · CRYSTAL STRUCTURE OF flagellar protein FlgA FROM Thermotoga maritima MSB8 · 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 Q9X1M7
- Elsewhere: RCSB PDB 3FRN · PDBe 3FRN · UniProt Q9X1M7
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