Research workbench
Structure of apo-dehydroascorbate reductase from pennisetum glaucum phased by iodide-sad method
Analyse Structure of apo-dehydroascorbate reductase from pennisetum glaucum phased by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5IQY
- Type
- protein
- Length
- 211 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dehydroascorbate reductase
- EC
- 1.8.5.1
- UniProt
- U5XYA0
- Ligands
- IOD
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dehydroascorbate reductase (EC 1.8.5.1) | protein | 211 | 53% helix, 10% strand | U5XYA0 |
Ligands and binding sites
- IOD · Iodide ion · ion · 26 copies · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.39 | 0.76 | 22 | IOD |
Compared structures
- 5IQY · Structure of apo-Dehydroascorbate Reductase from Pennisetum Glaucum phased by Iodide-SAD… · 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 U5XYA0
- Elsewhere: RCSB PDB 5IQY · PDBe 5IQY · UniProt U5XYA0
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