Research workbench
Crystal structure of aspergillus fumigatus EGA3
Analyse Crystal structure of aspergillus fumigatus EGA3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OJ1
- Type
- protein
- Length
- 251 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo alpha-1,4 polygalactosaminidase
- UniProt
- Q4WX16
- Ligands
- NAG, MAN, BMA, K
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo alpha-1,4 polygalactosaminidase | protein | 251 | 32% helix, 22% strand | Q4WX16 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 5 copies · chains A
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains A
- K · Potassium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 311 | 0.53 | 0.74 | 37 | K |
Modifications
Observed in the structure: 5 glycan, 3 disulfide (N-glycosylation, disulfide).
Compared structures
- 6OJ1 · Crystal Structure of Aspergillus fumigatus Ega3 · 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 Q4WX16
- Elsewhere: RCSB PDB 6OJ1 · PDBe 6OJ1 · UniProt Q4WX16
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