Research workbench
Solution structure of C20S variant of dehydroascorbate reductase 3A from populus trichocarpa in complex with dehydroascorbic acid.
Analyse Solution structure of C20S variant of dehydroascorbate reductase 3A from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MYE
- Type
- protein
- Length
- 212 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dehydroascorbate reductase family protein
- UniProt
- B9HM36
- Ligands
- UU3
- Pockets
- 2 · best druggability 0.46
Structure
solution nmr · 1 distinct chain · 48% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dehydroascorbate reductase family protein | protein | 212 | 48% helix, 10% strand | B9HM36 |
Ligands and binding sites
- UU3 · (5R)-5-[(1S)-1,2-bis(oxidanyl)ethyl]oxolane-2,3,4-trione · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.46 | 0.82 | 15 | empty |
| 2 | 110 | 0.46 | 0.78 | 21 | UU3 |
Compared structures
- 5MYE · Solution structure of C20S variant of Dehydroascorbate reductase 3A from Populus… · 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 B9HM36
- Elsewhere: RCSB PDB 5MYE · PDBe 5MYE · UniProt B9HM36
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