MolNFT v1 · #67533 · protein
Crystal structure of a FMN-binding protein (SWOL_0183) from syntrophomonas wolfei subsp. wolfei at 2.12 a resolution
3IN6: “Crystal structure of a FMN-binding protein (SWOL_0183) from syntrophomonas wolfei subsp. wolfei at 2.12 a…”. X-ray diffraction, 1 ligand (FMN), 2 pockets (best druggability 0.64). MolNFT v1 #67533 on GenesisL1: 3D structure, binding…
- PDB
- 3IN6
- Type
- protein
- Length
- 294 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FMN-binding protein
- UniProt
- Q0B0G9
- Ligands
- FMN
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | FMN-binding protein | protein | 147 | 35% helix, 38% strand | Q0B0G9 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 228 | 0.64 | 0.83 | 37 | FMN |
| 2 | 275 | 0.64 | 0.81 | 47 | FMN |
Interfaces
1 interface between chains.
- A–B · 1517 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 3IN6 · Crystal structure of a fmn-binding protein (swol_0183) from syntrophomonas wolfei subsp.… · 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 Q0B0G9
- Elsewhere: RCSB PDB 3IN6 · PDBe 3IN6 · UniProt Q0B0G9
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