Research workbench
Ribose 5-phosphate isomerase from plasmodium falciparum
Analyse Ribose 5-phosphate isomerase from plasmodium falciparum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F8M
- Type
- protein
- Length
- 472 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribose 5-phosphate isomerase
- EC
- 5.3.1.6
- UniProt
- Q8I3W2
- Ligands
- PO4
- Pockets
- 5 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribose 5-phosphate isomerase (EC 5.3.1.6) | protein | 237 | 30% helix, 26% strand | Q8I3W2 |
| B | Ribose 5-phosphate isomerase (EC 5.3.1.6) | protein | 235 | 29% helix, 26% strand | Q8I3W2 |
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
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 200 | 0.47 | 0.74 | 22 | empty |
| 2 | 192 | 0.47 | 0.75 | 21 | empty |
| 3 | 59 | 0.38 | 0.80 | 18 | PO4 |
| 4 | 60 | 0.37 | 0.80 | 21 | PO4 |
| 5 | 57 | 0.27 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1397 Ų buried · 11 hydrogen bonds · 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 Q8I3W2
- Elsewhere: RCSB PDB 2F8M · PDBe 2F8M · UniProt Q8I3W2
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