MolNFT v1 · #10377 · protein
Tropinone reductase-II complexed with NADPH and tropinone
1IPF: “Tropinone reductase-II complexed with NADPH and tropinone”. X-ray diffraction, 2 ligands (NDP, TNE), 5 pockets (best druggability 0.79). MolNFT v1 #10377 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1IPF
- Type
- protein
- Length
- 518 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tropinone reductase-II
- EC
- 1.1.1.236
- UniProt
- P50163
- Ligands
- NDP, TNE
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Tropinone reductase-II (EC 1.1.1.236) | protein | 259 | 51% helix, 15% strand | P50163 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- TNE · 8-methyl-8-azabicyclo[3,2,1]octan-3-one · 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 | 624 | 0.79 | 0.85 | 65 | NDP, TNE |
| 2 | 562 | 0.79 | 0.85 | 65 | NDP, TNE |
| 3 | 89 | 0.47 | 0.81 | 15 | empty |
| 4 | 117 | 0.45 | 0.78 | 21 | empty |
| 5 | 98 | 0.40 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1356 Ų buried · 13 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 1IPF · PDBe 1IPF · UniProt P50163
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