MolNFT v1 · #103878 · protein
Crystal structure of the escherichia COLI alkanesulfonate FMN reductase ssue in FMNH2-bound form
4PU0: “Crystal structure of the escherichia COLI alkanesulfonate FMN reductase ssue in FMNH2-bound form”. X-ray diffraction, 2 ligands (FMN, PO4), 9 pockets (best druggability 0.76). MolNFT v1 #103878 on GenesisL1: 3D structure, binding…
- PDB
- 4PU0
- Type
- protein
- Length
- 692 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FMN reductase ssue
- EC
- 1.5.1.38
- UniProt
- P80644
- Ligands
- FMN, PO4
- Pockets
- 9 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, A, B, D | FMN reductase ssue (EC 1.5.1.38) | protein | 173 | 45% helix, 24% strand | P80644 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 3 copies · chains C, A, B, D
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · 3 copies · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 368 | 0.76 | 0.86 | 51 | empty |
| 2 | 172 | 0.56 | 0.80 | 24 | GOL |
| 3 | 190 | 0.54 | 0.79 | 28 | GOL |
| 4 | 138 | 0.42 | 0.75 | 26 | FMN |
| 5 | 102 | 0.40 | 0.77 | 27 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1222 Ų buried · 18 hydrogen bonds · protein-protein
- C–A · 732 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 684 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 4PU0 · Crystal structure of the Escherichia coli alkanesulfonate FMN reductase SsuE in… · the same entry in another collection · chain C against C, TM-score 1.00
- P80644 · AlphaFold monomer V2.0 prediction for FMN reductase (NADPH) (P80644) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P80644
- Elsewhere: RCSB PDB 4PU0 · PDBe 4PU0 · UniProt P80644
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.