Research workbench
Joint X-ray neutron structure of cholesterol oxidase
Analyse Joint X-ray neutron structure of cholesterol oxidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KWF
- Type
- protein
- Length
- 498 residues
- Chains
- 1
- Method
- x-ray diffraction; neutron diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cholesterol oxidase
- EC
- 1.1.3.6, 5.3.3.1
- UniProt
- P12676
- Ligands
- FAD
- Pockets
- 4 · best druggability 0.86
Structure
x-ray diffraction; neutron diffraction · 1 distinct chain · 29% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cholesterol oxidase (EC 1.1.3.6, 5.3.3.1) | protein | 498 | 29% helix, 24% strand | P12676 |
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
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 | 853 | 0.86 | 0.88 | 89 | FAD |
| 2 | 132 | 0.45 | 0.77 | 24 | empty |
| 3 | 52 | 0.34 | 0.78 | 16 | empty |
| 4 | 76 | 0.33 | 0.75 | 23 | empty |
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 P12676
- Elsewhere: RCSB PDB 5KWF · PDBe 5KWF · UniProt P12676
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