MolNFT v1 · #62755 · protein
Crystal structure of phosphoglycerate mutase from plasmodium falciparum, PFD0660W
3EOZ · Putative phosphoglycerate mutase: “Crystal structure of phosphoglycerate mutase from plasmodium falciparum, PFD0660W”. X-ray diffraction, 1 ligand (PO4), 5 pockets (best druggability 0.73). MolNFT v1 #62755 on GenesisL1: 3D…
- PDB
- 3EOZ
- Type
- protein
- Length
- 334 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative phosphoglycerate mutase
- EC
- 5.4.2.1
- UniProt
- Q8I1V2
- Ligands
- PO4
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative phosphoglycerate mutase (EC 5.4.2.1) | protein | 159 | 39% helix, 26% strand | Q8I1V2 |
| B | Putative phosphoglycerate mutase (EC 5.4.2.1) | protein | 175 | 42% helix, 28% strand | Q8I1V2 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · 3 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 769 | 0.73 | 0.78 | 78 | PO4 |
| 2 | 170 | 0.61 | 0.83 | 23 | empty |
| 3 | 291 | 0.54 | 0.75 | 28 | empty |
| 4 | 80 | 0.45 | 0.81 | 16 | empty |
| 5 | 145 | 0.45 | 0.77 | 19 | GOL |
Interfaces
1 interface between chains.
- A–B · 1438 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 3EOZ · Crystal Structure of Phosphoglycerate Mutase from Plasmodium Falciparum, PFD0660w · 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 Q8I1V2
- Elsewhere: RCSB PDB 3EOZ · PDBe 3EOZ · UniProt Q8I1V2
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