Research workbench
Crystal structure of human inositol polyphosphate multikinase (ipmk) catalytic core domain
Analyse Crystal structure of human inositol polyphosphate multikinase (ipmk) catalytic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E7F
- Type
- protein
- Length
- 469 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
- Q8NFU5
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inositol polyphosphate multikinase (EC 2.7.1.151) | protein | 235 | 35% helix, 24% strand | Q8NFU5 |
| B | Inositol polyphosphate multikinase (EC 2.7.1.151) | protein | 234 | 37% helix, 24% strand | Q8NFU5 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 722 | 0.72 | 0.78 | 92 | empty |
| 2 | 369 | 0.61 | 0.77 | 46 | empty |
| 3 | 52 | 0.29 | 0.75 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 695 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 6E7F · Crystal Structure of Human Inositol Polyphosphate Multikinase (IPMK) Catalytic Core Domain · the same entry in another collection · chain A against A, TM-score 1.00
- Q8NFU5 · AlphaFold monomer V2.0 prediction for inositol polyphosphate multikinase (Q8NFU5) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q8NFU5
- Elsewhere: RCSB PDB 6E7F · PDBe 6E7F · UniProt Q8NFU5
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