Research workbench
Crystal structure of apo-form (P21) of dual activity FBPASE/IMPASE (AF2372) from archaeoglobus fulgidus
Analyse Crystal structure of apo-form (P21) of dual activity FBPASE/IMPASE (AF2372)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LBV
- 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 monophosphatase
- EC
- 3.1.3.11, 3.1.3.25
- UniProt
- O30298
- Pockets
- 6 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fructose 1,6-BISPHOSPHATASE/INOSITOL monophosphatase (EC 3.1.3.11, 3.1.3.25) | protein | 252 | 30% helix, 30% strand | O30298 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 651 | 0.76 | 0.82 | 58 | empty |
| 2 | 668 | 0.74 | 0.81 | 57 | empty |
| 3 | 118 | 0.36 | 0.73 | 15 | empty |
| 4 | 107 | 0.35 | 0.73 | 14 | empty |
| 5 | 63 | 0.27 | 0.73 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1241 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 1LBV · Crystal Structure of apo-form (P21) of dual activity FBPase/IMPase (AF2372) from… · the same entry in another collection · chain A against A, TM-score 1.00
- O30298 · AlphaFold monomer V2.0 prediction for fructose-1,6-BISPHOSPHATASE/INOSITOL-1-monophosphata… · a predicted model of the same protein · chain B against A, TM-score 0.99
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 1LBV · PDBe 1LBV · UniProt O30298
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.