Research workbench
RV3094C in complex with FAD and eth.
Analyse RV3094C in complex with FAD and eth. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7F72
- Type
- protein
- Length
- 370 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RV3094C
- UniProt
- O05773
- Ligands
- 1JA, FMN
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RV3094C | protein | 370 | 58% helix, 15% strand | O05773 |
Ligands and binding sites
- 1JA · 2-ethylpyridine-4-carboximidothioic acid · ligand · chains A
- FMN · Flavin mononucleotide · ligand · chains 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 | 105 | 0.56 | 0.84 | 21 | FMN |
| 2 | 149 | 0.50 | 0.78 | 26 | 1JA |
| 3 | 134 | 0.48 | 0.78 | 19 | empty |
Compared structures
- 7F72 · Rv3094c in complex with FAD and ETH. · 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 O05773
- Elsewhere: RCSB PDB 7F72 · PDBe 7F72 · UniProt O05773
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.