Research workbench
Crystal structure of S-nitrosoglutathione reductase from arabidopsis thaliana, complex with NADH
Analyse Crystal structure of S-nitrosoglutathione reductase from arabidopsis thaliana… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UKO
- Type
- protein
- Length
- 756 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alcohol dehydrogenase class-3
- EC
- 1.1.1.1, 1.1.1.-, 1.1.1.284
- UniProt
- Q96533
- Ligands
- NAD, ZN, SO4
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Alcohol dehydrogenase class-3 (EC 1.1.1.1, 1.1.1.-, 1.1.1.284) | protein | 378 | 30% helix, 25% strand | Q96533 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 4 copies · chains A, B
- SO4 · Sulfate ion · ion · 12 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 959 | 0.77 | 0.80 | 83 | SO4, NAD |
| 2 | 1071 | 0.77 | 0.79 | 91 | NAD, SO4 |
| 3 | 485 | 0.63 | 0.76 | 56 | SO4 |
Interfaces
1 interface between chains.
- A–B · 1489 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 3UKO · Crystal Structure of S-Nitrosoglutathione Reductase from Arabidopsis thaliana, complex… · the same entry in another collection · chain A against A, TM-score 1.00
- Q96533 · AlphaFold monomer V2.0 prediction for alcohol dehydrogenase class-3 (Q96533) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q96533
- Elsewhere: RCSB PDB 3UKO · PDBe 3UKO · UniProt Q96533
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.