MolNFT v1 · #111636 · protein
Crystal structure of NADH-FMN oxidoreductase from mycobacterium avium
4YWN: “Crystal structure of NADH-FMN oxidoreductase from mycobacterium avium”. X-ray diffraction, 1 pocket (best druggability 0.56). MolNFT v1 #111636 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4YWN
- Type
- protein
- Length
- 279 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADH-FMN oxidoreductase
- UniProt
- A0QM95
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-FMN oxidoreductase | protein | 138 | 14% helix, 54% strand | A0QM95 |
| B | NADH-FMN oxidoreductase | protein | 141 | 13% helix, 52% strand | A0QM95 |
Ligands and binding sites
- FLC · Citrate anion · 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 | 129 | 0.56 | 0.82 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1618 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 4YWN · Crystal structure of NADH-FMN oxidoreductase from Mycobacterium avium · the same entry in another collection · chain B against B, 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 A0QM95
- Elsewhere: RCSB PDB 4YWN · PDBe 4YWN · UniProt A0QM95
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