Research workbench
Crystal structure of Q64E mutant of triosephosphate isomerase from plasmodium falciparum
Analyse Crystal structure of Q64E mutant of triosephosphate isomerase from plasmodium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5BRB
- Type
- protein
- Length
- 486 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- Q07412
- Ligands
- NA
- Pockets
- 5 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triosephosphate isomerase (EC 5.3.1.1) | protein | 243 | 41% helix, 17% strand | Q07412 |
| B | Triosephosphate isomerase (EC 5.3.1.1) | protein | 243 | 45% helix, 17% strand | Q07412 |
Ligands and binding sites
- NA · Sodium ion · metal · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 127 | 0.76 | 0.95 | 32 | empty |
| 2 | 254 | 0.64 | 0.82 | 41 | empty |
| 3 | 133 | 0.44 | 0.77 | 22 | empty |
| 4 | 82 | 0.43 | 0.80 | 20 | empty |
| 5 | 50 | 0.38 | 0.80 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1546 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 5BRB · Crystal structure of Q64E mutant of Triosephosphate isomerase from Plasmodium falciparum · 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 5BRB · PDBe 5BRB · UniProt Q07412
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