Research workbench
The crystal structure of human isopentenyl diphophate isomerase
Analyse The crystal structure of human isopentenyl diphophate isomerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ICJ
- Type
- protein
- Length
- 219 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isopentenyl-diphosphate delta isomerase
- EC
- 5.3.3.2
- UniProt
- Q86U81
- Ligands
- MG, SO4
- Pockets
- 1 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isopentenyl-diphosphate delta isomerase (EC 5.3.3.2) | protein | 219 | 33% helix, 31% strand | Q86U81 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 67 | 0.72 | 0.98 | 22 | SO4 |
Compared structures
- 2ICJ · The crystal structure of human isopentenyl diphophate isomerase · 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 Q86U81
- Elsewhere: RCSB PDB 2ICJ · PDBe 2ICJ · UniProt Q86U81
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