Research workbench
Crystallographic analysis of the complex between triosephosphate isomerase from trypanosoma cruzi and 3-(2-benzothiazolylthio)-1- propanesulfonic acid
Analyse Crystallographic analysis of the complex between triosephosphate isomerase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SUX
- Type
- protein
- Length
- 500 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase, glycosomal
- EC
- 5.3.1.1
- UniProt
- P52270
- Ligands
- BTS, SO4
- Pockets
- 5 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Triosephosphate isomerase, glycosomal (EC 5.3.1.1) | protein | 250 | 47% helix, 17% strand | P52270 |
Ligands and binding sites
- BTS · 3-(2-benzothiazolylthio)-1-propanesulfonic acid · ligand · chains A, B
- SO4 · Sulfate ion · ion · 7 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 | 97 | 0.39 | 0.76 | 17 | empty |
| 2 | 73 | 0.38 | 0.77 | 14 | empty |
| 3 | 83 | 0.35 | 0.76 | 26 | SO4 |
| 4 | 66 | 0.35 | 0.78 | 24 | SO4 |
| 5 | 51 | 0.29 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1519 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 1SUX · CRYSTALLOGRAPHIC ANALYSIS OF THE COMPLEX BETWEEN TRIOSEPHOSPHATE ISOMERASE FROM… · the same entry in another collection · chain A against A, TM-score 1.00
- P52270 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase, glycosomal (P52270) · 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 P52270
- Elsewhere: RCSB PDB 1SUX · PDBe 1SUX · UniProt P52270
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