Research workbench
Imine Reductase from Rhodococcus erythropolis
Analyse Imine Reductase from Rhodococcus erythropolis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 9FM7
- Type
- protein
- Length
- 286 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Rhodococcus erythropolis
- Molecule
- NAD(P)-dependent oxidoreductase
- UniProt
- A0A3G9A570
- Ligands
- ATR
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 57% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)-dependent oxidoreductase | protein | 286 | 57% helix, 13% strand | A0A3G9A570 |
Ligands and binding sites
- ATR · 2'-monophosphoadenosine-5'-diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 710 | 0.65 | 0.74 | 39 | empty |
| 2 | 98 | 0.34 | 0.73 | 15 | empty |
| 3 | 68 | 0.34 | 0.76 | 14 | empty |
| 4 | 87 | 0.34 | 0.74 | 19 | ATR |
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 A0A3G9A570
- Elsewhere: RCSB PDB 9FM7 · PDBe 9FM7 · UniProt A0A3G9A570
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