Research workbench
Structural studies and protein engineering of inositol phosphate multikinase
Analyse Structural studies and protein engineering of inositol phosphate multikinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FRF
- Type
- protein
- Length
- 427 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inositol polyphosphate multikinase alpha
- EC
- 2.7.1.140, 2.7.1.151
- UniProt
- Q9LY23
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inositol polyphosphate multikinase alpha (EC 2.7.1.140, 2.7.1.151) | protein | 214 | 39% helix, 19% strand | Q9LY23 |
| B | Inositol polyphosphate multikinase alpha (EC 2.7.1.140, 2.7.1.151) | protein | 213 | 38% helix, 21% strand | Q9LY23 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 158 | 0.57 | 0.81 | 28 | empty |
| 2 | 94 | 0.49 | 0.82 | 21 | SO4 |
| 3 | 96 | 0.45 | 0.79 | 20 | SO4 |
| 4 | 83 | 0.32 | 0.73 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1056 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 4FRF · Structural Studies and Protein Engineering of Inositol Phosphate Multikinase · the same entry in another collection · chain A against A, TM-score 1.00
- Q9LY23 · AlphaFold monomer V2.0 prediction for inositol polyphosphate multikinase alpha (Q9LY23) · 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 Q9LY23
- Elsewhere: RCSB PDB 4FRF · PDBe 4FRF · UniProt Q9LY23
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