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Crystal structure of DBR2
Analyse Crystal structure of DBR2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DY3
- Type
- protein
- Length
- 374 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Artemisinic aldehyde DELTA(11(13)) reductase
- EC
- 1.3.1.92
- UniProt
- C5H429
- Ligands
- FMN, HBA
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Artemisinic aldehyde DELTA(11(13)) reductase (EC 1.3.1.92) | protein | 374 | 39% helix, 14% strand | C5H429 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · chains A
- HBA · P-hydroxybenzaldehyde · ligand · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 585 | 0.71 | 0.79 | 44 | FMN, HBA |
| 2 | 86 | 0.48 | 0.82 | 15 | empty |
| 3 | 80 | 0.34 | 0.75 | 15 | empty |
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 C5H429
- Elsewhere: RCSB PDB 5DY3 · PDBe 5DY3 · UniProt C5H429
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