Research workbench
Crystal structure of inositol phosphate multikinase IPK2 from S. cerevisiae
Analyse Crystal structure of inositol phosphate multikinase IPK2 from S. cerevisiae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IEW
- Type
- protein
- Length
- 514 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inositol polyphosphate multikinase
- EC
- 2.7.1.151
- UniProt
- P07250
- Ligands
- CA
- Pockets
- 8 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inositol polyphosphate multikinase (EC 2.7.1.151) | protein | 258 | 40% helix, 23% strand | P07250 |
| B | Inositol polyphosphate multikinase (EC 2.7.1.151) | protein | 256 | 39% helix, 23% strand | P07250 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 122 | 0.48 | 0.79 | 15 | empty |
| 2 | 172 | 0.47 | 0.75 | 23 | empty |
| 3 | 141 | 0.45 | 0.76 | 23 | empty |
| 4 | 56 | 0.45 | 0.83 | 15 | empty |
| 5 | 91 | 0.44 | 0.80 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 915 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 2IEW · Crystal structure of Inositol Phosphate Multikinase Ipk2 from S. cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
- P07250 · AlphaFold monomer V2.0 prediction for inositol polyphosphate multikinase (P07250) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P07250
- Elsewhere: RCSB PDB 2IEW · PDBe 2IEW · UniProt P07250
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