Research workbench
The crystal structure of flavin reductase hpac complexed with NADP+
Analyse The crystal structure of flavin reductase hpac complexed with NADP+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2D38
- Type
- protein
- Length
- 156 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical NADH-dependent FMN oxidoreductase
- EC
- 1.6.8.-
- Ligands
- FMN, NAP
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical NADH-dependent FMN oxidoreductase (EC 1.6.8.-) | protein | 156 | 19% helix, 49% strand | — |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · chains A
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 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 | 330 | 0.55 | 0.75 | 38 | FMN, NAP |
Compared structures
- 2D38 · The Crystal Structure of Flavin Reductase HpaC complexed with NADP+ · 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
- Elsewhere: RCSB PDB 2D38 · PDBe 2D38
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