Research workbench
Dehydroascorbate reductase 3A from populus trichocarpa complexed with gsh.
Analyse Dehydroascorbate reductase 3A from populus trichocarpa complexed with gsh. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5N9U
- 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
- GSH
- Pockets
- 3 · best druggability 0.48
Structure
solution nmr · 1 distinct chain · 50% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dehydroascorbate reductase family protein | protein | 212 | 50% helix, 11% strand | B9HM36 |
Ligands and binding sites
- GSH · Glutathione · ligand · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 101 | 0.48 | 0.80 | 19 | GSH |
| 2 | 66 | 0.47 | 0.83 | 16 | empty |
| 3 | 50 | 0.29 | 0.76 | 19 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 5N9U · Dehydroascorbate reductase 3A from Populus trichocarpa complexed with GSH. · 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 5N9U · PDBe 5N9U · UniProt B9HM36
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