Research workbench
Tropinone reductase-II complexed with NADP+ and pseudotropine
Analyse Tropinone reductase-II complexed with NADP+ and pseudotropine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AE2
- Type
- protein
- Length
- 518 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (tropinone reductase-II)
- EC
- 1.1.1.236
- UniProt
- P50163
- Ligands
- NAP, PTO
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (tropinone reductase-II) (EC 1.1.1.236) | protein | 259 | 51% helix, 16% strand | P50163 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- PTO · Pseudotropine · ligand · 2 copies · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 562 | 0.79 | 0.85 | 66 | NAP, PTO |
| 2 | 622 | 0.79 | 0.84 | 65 | NAP, PTO |
| 3 | 137 | 0.49 | 0.79 | 27 | empty |
| 4 | 57 | 0.42 | 0.82 | 13 | empty |
| 5 | 76 | 0.36 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1374 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
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 P50163
- Elsewhere: RCSB PDB 2AE2 · PDBe 2AE2 · UniProt P50163
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