Research workbench
Impase (AF2372) with 25 mm asp
Analyse Impase (AF2372) with 25 mm asp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6B64
- Type
- protein
- Length
- 504 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-1,6-BISPHOSPHATASE/INOSITOL-1-monophosphatase
- EC
- 3.1.3.11, 3.1.3.25
- UniProt
- O30298
- Ligands
- ASP, MG, SO4
- Pockets
- 5 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fructose-1,6-BISPHOSPHATASE/INOSITOL-1-monophosphatase (EC 3.1.3.11, 3.1.3.25) | protein | 252 | 30% helix, 29% strand | O30298 |
Ligands and binding sites
- ASP · Aspartic acid · ligand · 8 copies · chains A, B
- MG · Magnesium ion · metal · 6 copies · chains A, B
- SO4 · Sulfate ion · ion · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 398 | 0.69 | 0.82 | 42 | ASP, SO4 |
| 2 | 426 | 0.68 | 0.80 | 42 | ASP, SO4, MG |
| 3 | 110 | 0.40 | 0.76 | 21 | empty |
| 4 | 69 | 0.34 | 0.76 | 20 | empty |
| 5 | 56 | 0.24 | 0.72 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1240 Ų buried · 9 hydrogen bonds · protein-protein
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 O30298
- Elsewhere: RCSB PDB 6B64 · PDBe 6B64 · UniProt O30298
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