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Crystal structure of dehydrogenase domain of cylindrospermum stagnale NADPH-oxidase 5 (NOX5)
Analyse Crystal structure of dehydrogenase domain of cylindrospermum stagnale… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5O0X
- Type
- protein
- Length
- 261 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- K9WT99
- Ligands
- FAD, CL
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 261 | — | K9WT99 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- CL · Chloride ion · ion · 7 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 9 copies · chains A
- GOL · Glycerol · additive · 6 copies · chains A
- P6G · Hexaethylene glycol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5O0X · Crystal structure of dehydrogenase domain of Cylindrospermum stagnale NADPH-Oxidase 5… · 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 K9WT99
- Elsewhere: RCSB PDB 5O0X · PDBe 5O0X · UniProt K9WT99
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