Research workbench
Crystal structure of a ternary complex of dual activity FBPASE/IMPASE (AF2372) from archaeoglobus fulgidus with calcium ions and D-myo-inositol-1-phosphate
Analyse Crystal structure of a ternary complex 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
- 1LBX
- 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
- Ligands
- IPD, CA
- Pockets
- 5 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 27% 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 | 32% helix, 27% strand | O30298 |
Ligands and binding sites
- IPD · D-myo-inositol-1-phosphate · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · 4 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 | 641 | 0.70 | 0.79 | 59 | CA, IPD |
| 2 | 484 | 0.67 | 0.79 | 42 | CA, IPD |
| 3 | 68 | 0.33 | 0.75 | 16 | empty |
| 4 | 72 | 0.28 | 0.73 | 14 | empty |
| 5 | 56 | 0.25 | 0.73 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1229 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 1LBX · Crystal Structure of a ternary complex 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 1LBX · PDBe 1LBX · UniProt O30298
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