Research workbench
IPP:DMAPP isomerase type II, FMN complex
Analyse IPP:DMAPP isomerase type II, FMN complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1P0N
- Type
- protein
- Length
- 612 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
- FMN
- Pockets
- 6 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isopentenyl-diphosphate delta-isomerase (EC 5.3.3.2) | protein | 305 | 47% helix, 16% strand | P50740 |
| B | Isopentenyl-diphosphate delta-isomerase (EC 5.3.3.2) | protein | 307 | 49% helix, 16% strand | P50740 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 145 | 0.42 | 0.74 | 24 | empty |
| 2 | 156 | 0.42 | 0.74 | 28 | FMN |
| 3 | 138 | 0.40 | 0.74 | 19 | empty |
| 4 | 111 | 0.36 | 0.74 | 26 | FMN |
| 5 | 69 | 0.31 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 579 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 1P0N · PDBe 1P0N · UniProt P50740
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