Research workbench
Crystal structures of NADH:FMN oxidoreductase (emob) - apo form
Analyse Crystal structures of NADH:FMN oxidoreductase (emob) - apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LTD
- Type
- protein
- Length
- 187 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADH-dependent FMN reductase
- EC
- 1.5.1.42
- UniProt
- Q9F9T2
- Ligands
- SO4, PO4
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-dependent FMN reductase (EC 1.5.1.42) | protein | 187 | 44% helix, 21% strand | Q9F9T2 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 4LTD · Crystal structures of NADH:FMN oxidoreductase (EMOB) - apo form · 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 Q9F9T2
- Elsewhere: RCSB PDB 4LTD · PDBe 4LTD · UniProt Q9F9T2
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