Research workbench
Crystal structure of selenomonas ruminantium phytase complexed with persulfated phytate
Analyse Crystal structure of selenomonas ruminantium phytase complexed with persulfated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1U26
- Type
- protein
- Length
- 627 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myo-inositol hexaphosphate phosphohydrolase
- EC
- 3.1.3.72
- UniProt
- Q7WUJ1
- Ligands
- IHS
- Pockets
- 6 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myo-inositol hexaphosphate phosphohydrolase (EC 3.1.3.72) | protein | 314 | 40% helix, 18% strand | Q7WUJ1 |
| B | Myo-inositol hexaphosphate phosphohydrolase (EC 3.1.3.72) | protein | 313 | 38% helix, 18% strand | Q7WUJ1 |
Ligands and binding sites
- IHS · D-myo-inositol-hexasulphate · ligand · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1063 | 0.74 | 0.77 | 106 | IHS |
| 2 | 371 | 0.60 | 0.76 | 50 | IHS |
| 3 | 311 | 0.59 | 0.77 | 43 | IHS |
| 4 | 51 | 0.40 | 0.82 | 13 | empty |
| 5 | 54 | 0.28 | 0.74 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 407 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1U26 · Crystal structure of Selenomonas ruminantium phytase complexed with persulfated phytate · 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 Q7WUJ1
- Elsewhere: RCSB PDB 1U26 · PDBe 1U26 · UniProt Q7WUJ1
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