Research workbench
Structure of flavin-containing monooxygenase from cellvibrio sp. br
Analyse Structure of flavin-containing monooxygenase from cellvibrio sp. br in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4USQ
- Type
- protein
- Length
- 674 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pyridine nucleotide-disulfide oxidoreductase
- EC
- 1.14.13.8
- UniProt
- I3IEE4
- Ligands
- FAD
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pyridine nucleotide-disulfide oxidoreductase (EC 1.14.13.8) | protein | 333 | 29% helix, 22% strand | I3IEE4 |
| F | Pyridine nucleotide-disulfide oxidoreductase (EC 1.14.13.8) | protein | 341 | 29% helix, 21% strand | I3IEE4 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 984 | 0.80 | 0.82 | 98 | FAD |
| 2 | 961 | 0.80 | 0.82 | 104 | FAD |
| 3 | 146 | 0.67 | 0.88 | 27 | empty |
| 4 | 158 | 0.58 | 0.82 | 32 | empty |
| 5 | 158 | 0.54 | 0.80 | 28 | empty |
Interfaces
1 interface between chains.
- A–F · 1264 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 4USQ · Structure of flavin-containing monooxygenase from Cellvibrio sp. BR · 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 I3IEE4
- Elsewhere: RCSB PDB 4USQ · PDBe 4USQ · UniProt I3IEE4
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