Research workbench
Triosephosphate isomerase from gallus gallus, loop 6 hinge mutant K174L, T175W
Analyse Triosephosphate isomerase from gallus gallus, loop 6 hinge mutant K174L, T175W in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SW0
- Type
- protein
- Length
- 494 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- P00940
- Ligands
- PGA
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Triosephosphate isomerase (EC 5.3.1.1) | protein | 247 | 44% helix, 17% strand | P00940 |
Ligands and binding sites
- PGA · 2-phosphoglycolic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.72 | 0.97 | 26 | empty |
| 2 | 68 | 0.43 | 0.81 | 25 | PGA |
| 3 | 55 | 0.41 | 0.82 | 19 | PGA |
| 4 | 54 | 0.34 | 0.78 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1669 Ų buried · 29 hydrogen bonds · protein-protein
Compared structures
- 1SW0 · Triosephosphate isomerase from Gallus gallus, loop 6 hinge mutant K174L, T175W · the same entry in another collection · chain A against A, TM-score 1.00
- P00940 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase (P00940) · 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 P00940
- Elsewhere: RCSB PDB 1SW0 · PDBe 1SW0 · UniProt P00940
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