MolNFT v1 · #38160 · protein
Structure of wild type, oxidized SYE1, an oye homologue from S. oneidensis
2GOU · Oxidoreductase, FMN-binding: “Structure of wild type, oxidized SYE1, an oye homologue from S. oneidensis”. X-ray diffraction, 2 ligands (FMN, SO4), 1 pocket (best druggability 0.77). MolNFT v1 #38160 on GenesisL1: 3D structure…
- PDB
- 2GOU
- Type
- protein
- Length
- 365 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Oxidoreductase, FMN-binding
- UniProt
- Q8EEC8
- Ligands
- FMN, SO4
- Pockets
- 1 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oxidoreductase, FMN-binding | protein | 365 | 36% helix, 18% strand | Q8EEC8 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
- BOG · octyl beta-D-glucopyranoside · additive · chains A
- PE4 · 2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-ethanol · additive · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 344 | 0.77 | 0.87 | 43 | FMN, PE4 |
Compared structures
- 2GOU · Structure of wild type, oxidized SYE1, an OYE homologue from S. oneidensis · 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 Q8EEC8
- Elsewhere: RCSB PDB 2GOU · PDBe 2GOU · UniProt Q8EEC8
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