Research workbench
Structure of a LOOP6 hinge mutant of plasmodium falciparum triosephosphate isomerase, W168F, complexed to sulfate
Analyse Structure of a LOOP6 hinge mutant of plasmodium falciparum triosephosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WOB
- Type
- protein
- Length
- 984 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- Q07412
- Ligands
- SO4
- Pockets
- 9 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Triosephosphate isomerase (EC 5.3.1.1) | protein | 246 | 44% helix, 16% strand | Q07412 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.76 | 0.98 | 26 | empty |
| 2 | 98 | 0.76 | 0.97 | 26 | empty |
| 3 | 85 | 0.57 | 0.87 | 23 | empty |
| 4 | 84 | 0.56 | 0.86 | 23 | empty |
| 5 | 81 | 0.44 | 0.80 | 20 | SO4 |
Interfaces
2 interfaces between chains.
- C–D · 1752 Ų buried · 32 hydrogen bonds · protein-protein
- A–B · 1746 Ų buried · 32 hydrogen bonds · protein-protein
Compared structures
- 1WOB · Structure of a loop6 hinge mutant of Plasmodium falciparum Triosephosphate Isomerase… · the same entry in another collection · chain A against A, TM-score 1.00
- Q07412 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase (Q07412) · a predicted model of the same protein · 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 Q07412
- Elsewhere: RCSB PDB 1WOB · PDBe 1WOB · UniProt Q07412
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