Research workbench
Binding of coumarins to NAD(P)H:FMN oxidoreductase
Analyse Binding of coumarins to NAD(P)H:FMN oxidoreductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1V5Z
- Type
- protein
- Length
- 434 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major NAD(P)H-flavin oxidoreductase
- EC
- 1.6.99.-
- UniProt
- P46072
- Ligands
- FMN, 2HC
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Major NAD(P)H-flavin oxidoreductase (EC 1.6.99.-) | protein | 217 | 47% helix, 16% strand | P46072 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- 2HC · (2E)-3-(2-hydroxyphenyl)acrylic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1163 | 0.82 | 0.83 | 116 | FMN, 2HC |
| 2 | 50 | 0.37 | 0.81 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 3474 Ų buried · 61 hydrogen bonds · protein-protein
Compared structures
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 P46072
- Elsewhere: RCSB PDB 1V5Z · PDBe 1V5Z · UniProt P46072
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