Research workbench
Crystallographic snapshots of aspergillus fumigatus phytase revealing its enzymatic dynamics
Analyse Crystallographic snapshots of aspergillus fumigatus phytase revealing its… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SK9
- Type
- protein
- Length
- 435 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-phytase a
- EC
- 3.1.3.8
- UniProt
- O00092
- Ligands
- NAG, PO4
- Pockets
- 3 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-phytase a (EC 3.1.3.8) | protein | 435 | 43% helix, 13% strand | O00092 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 376 | 0.60 | 0.77 | 42 | PO4 |
| 2 | 107 | 0.40 | 0.76 | 24 | empty |
| 3 | 56 | 0.28 | 0.74 | 16 | NAG |
Modifications
Observed in the structure: 5 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
- 1SK9 · Crystallographic snapshots of Aspergillus fumigatus phytase revealing its enzymatic… · the same entry in another collection · chain A against A, TM-score 1.00
- O00092 · AlphaFold monomer V2.0 prediction for 3-phytase a (O00092) · a predicted model of the same protein · 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 O00092
- Elsewhere: RCSB PDB 1SK9 · PDBe 1SK9 · UniProt O00092
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