Research workbench
Aspergillus niger phytase in complex with myo-inositol hexakis sulfate
Analyse Aspergillus niger phytase in complex with myo-inositol hexakis sulfate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3K4Q
- Type
- protein
- Length
- 876 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-phytase a
- EC
- 3.1.3.8
- UniProt
- P34752
- Ligands
- IHS, NAG
- Pockets
- 4 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 3-phytase a (EC 3.1.3.8) | protein | 438 | 44% helix, 13% strand | P34752 |
Ligands and binding sites
- IHS · D-myo-inositol-hexasulphate · ligand · 2 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 299 | 0.54 | 0.75 | 36 | IHS |
| 2 | 214 | 0.51 | 0.76 | 25 | empty |
| 3 | 259 | 0.51 | 0.75 | 30 | IHS |
| 4 | 168 | 0.46 | 0.76 | 25 | empty |
Modifications
Observed in the structure: 10 disulfide, 8 glycan (disulfide, N-glycosylation).
Compared structures
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 P34752
- Elsewhere: RCSB PDB 3K4Q · PDBe 3K4Q · UniProt P34752
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