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Crystal structure of the catalytic domain of human inositol 1,4,5- trisphosphate 3-kinase C
Analyse Crystal structure of the catalytic domain of human inositol 1,4,5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A98
- Type
- protein
- Length
- 259 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inositol 1,4,5-trisphosphate 3-kinase C
- EC
- 2.7.1.127
- UniProt
- Q9Y475
- Ligands
- I3P
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inositol 1,4,5-trisphosphate 3-kinase C (EC 2.7.1.127) | protein | 259 | 37% helix, 21% strand | Q9Y475 |
Ligands and binding sites
- I3P · D-myo-inositol-1,4,5-triphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 98 | 0.40 | 0.76 | 16 | empty |
| 2 | 91 | 0.33 | 0.73 | 22 | I3P |
Compared structures
- 2A98 · Crystal structure of the catalytic domain of human inositol 1,4,5-trisphosphate 3-kinase C · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9Y475
- Elsewhere: RCSB PDB 2A98 · PDBe 2A98 · UniProt Q9Y475
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