Research workbench
The structure of fsqb from aspergillus fumigatus, a flavoenzyme of the amine oxidase family
Analyse The structure of fsqb from aspergillus fumigatus, a flavoenzyme of the amine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GG2
- Type
- protein
- Length
- 494 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amino acid oxidase fmpa
- EC
- 1.5.3.-
- UniProt
- Q4WD43
- Ligands
- FAD
- Pockets
- 6 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amino acid oxidase fmpa (EC 1.5.3.-) | protein | 494 | 32% helix, 22% strand | Q4WD43 |
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
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 813 | 0.86 | 0.89 | 93 | FAD |
| 2 | 247 | 0.53 | 0.76 | 34 | empty |
| 3 | 127 | 0.39 | 0.74 | 20 | empty |
| 4 | 68 | 0.36 | 0.77 | 16 | empty |
| 5 | 63 | 0.35 | 0.77 | 18 | empty |
Modifications
Observed in the structure: 1 cofactor (flavinylation).
Compared structures
- 6GG2 · The structure of FsqB from Aspergillus fumigatus, a flavoenzyme of the amine oxidase… · the same entry in another collection · chain A against A, TM-score 1.00
- Q4WD43 · AlphaFold monomer V2.0 prediction for amino acid oxidase fsqb (Q4WD43) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q4WD43
- Elsewhere: RCSB PDB 6GG2 · PDBe 6GG2 · UniProt Q4WD43
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