Research workbench
Crystal structure of Cyclohexylamine Oxidase from Erythrobacteraceae bacterium
Analyse Crystal structure of Cyclohexylamine Oxidase from Erythrobacteraceae bacterium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LQC
- Type
- protein
- Length
- 450 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.88
- Source
- Erythrobacteraceae bacterium
- Molecule
- Cyclohexylamine Oxidase
- Ligands
- FAD
- Pockets
- 2 · best druggability 0.86
Structure
x-ray diffraction · resolution 1.88 · 1 distinct chain · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclohexylamine Oxidase | protein | 450 | 39% helix, 22% strand | — |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 412 | 0.86 | 0.94 | 62 | FAD |
| 2 | 125 | 0.52 | 0.80 | 16 | empty |
Compared structures
- 6LQC · Crystal structure of cyclohexylamine oxidase from erythrobacteraceae bacterium · 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
- Elsewhere: RCSB PDB 6LQC · PDBe 6LQC
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