Research workbench
IPP:DMAPP isomerase type II apo structure
Analyse IPP:DMAPP isomerase type II apo structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1P0K
- Type
- protein
- Length
- 615 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isopentenyl-diphosphate delta-isomerase
- EC
- 5.3.3.2
- UniProt
- P50740
- Ligands
- PO4
- Pockets
- 7 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isopentenyl-diphosphate delta-isomerase (EC 5.3.3.2) | protein | 306 | 47% helix, 17% strand | P50740 |
| B | Isopentenyl-diphosphate delta-isomerase (EC 5.3.3.2) | protein | 309 | 50% helix, 16% strand | P50740 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 151 | 0.55 | 0.81 | 30 | empty |
| 2 | 147 | 0.43 | 0.75 | 24 | empty |
| 3 | 153 | 0.43 | 0.74 | 24 | empty |
| 4 | 114 | 0.43 | 0.77 | 21 | empty |
| 5 | 173 | 0.42 | 0.74 | 33 | PO4 |
Interfaces
1 interface between chains.
- A–B · 519 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
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 P50740
- Elsewhere: RCSB PDB 1P0K · PDBe 1P0K · UniProt P50740
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