Research workbench
Structure of C126S mutant of saccharomyces cerevisiae triosephosphate isomerase
Analyse Structure of C126S mutant of saccharomyces cerevisiae triosephosphate isomerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FF7
- 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
- P00942
- Ligands
- PGA, NA, PO4, SO4
- Pockets
- 2 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Triosephosphate isomerase (EC 5.3.1.1) | protein | 247 | 45% helix, 17% strand | P00942 |
Ligands and binding sites
- PGA · 2-phosphoglycolic acid · ligand · chains A
- NA · Sodium ion · metal · chains A
- PO4 · Phosphate ion · ion · 3 copies · chains B
- SO4 · Sulfate ion · ion · 2 copies · chains B
- GOL · Glycerol · additive · 12 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 112 | 0.44 | 0.78 | 29 | SO4, GOL |
| 2 | 63 | 0.37 | 0.79 | 26 | PGA, NA |
Interfaces
1 interface between chains.
- A–B · 1727 Ų buried · 34 hydrogen bonds · protein-protein
Compared structures
- 4FF7 · Structure of C126S mutant of Saccharomyces cerevisiae triosephosphate isomerase · the same entry in another collection · chain A against A, TM-score 1.00
- P00942 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase (P00942) · 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 P00942
- Elsewhere: RCSB PDB 4FF7 · PDBe 4FF7 · UniProt P00942
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