Research workbench
Imine reductase from amycolatopsis orientalis. closed form in in complex with (R)- methyltetrahydroisoquinoline
Analyse Imine reductase from amycolatopsis orientalis. closed form in in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FWN
- Type
- protein
- Length
- 564 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Imine reductase
- EC
- 1.5.1.48
- UniProt
- R4SNK4
- Ligands
- NAP, YLG, SO4
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 56% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Imine reductase (EC 1.5.1.48) | protein | 282 | 55% helix, 12% strand | R4SNK4 |
| B | Imine reductase (EC 1.5.1.48) | protein | 282 | 57% helix, 12% strand | R4SNK4 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- YLG · (1R)-1-methyl-1,2,3,4-tetrahydroisoquinoline · ligand · chains A, B
- SO4 · Sulfate ion · ion · 4 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 | 85 | 0.71 | 0.95 | 20 | empty |
| 2 | 403 | 0.70 | 0.82 | 50 | NAP, YLG |
| 3 | 409 | 0.70 | 0.81 | 38 | empty |
Interfaces
1 interface between chains.
- A–B · 4276 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 5FWN · Imine Reductase from Amycolatopsis orientalis. Closed form in in complex with (R)… · 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 R4SNK4
- Elsewhere: RCSB PDB 5FWN · PDBe 5FWN · UniProt R4SNK4
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