Research workbench
Sinapyl alcohol dehydrogenase complexed with NADP+
Analyse Sinapyl alcohol dehydrogenase complexed with NADP+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YQD
- Type
- protein
- Length
- 718 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sinapyl alcohol dehydrogenase
- EC
- 1.1.1.195
- UniProt
- Q94G59
- Ligands
- NAP, ZN
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Sinapyl alcohol dehydrogenase (EC 1.1.1.195) | protein | 359 | 30% helix, 28% strand | Q94G59 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 4 copies · chains A, B
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · 2 copies · chains A, B
- GOL · Glycerol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 666 | 0.79 | 0.84 | 70 | NAP, DTT |
| 2 | 655 | 0.78 | 0.83 | 67 | NAP, DTT, GOL |
| 3 | 51 | 0.69 | 0.98 | 16 | empty |
| 4 | 56 | 0.69 | 0.97 | 15 | empty |
| 5 | 89 | 0.36 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1388 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 1YQD · Sinapyl Alcohol Dehydrogenase complexed with NADP+ · 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 Q94G59
- Elsewhere: RCSB PDB 1YQD · PDBe 1YQD · UniProt Q94G59
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