Research workbench
Triosephosphate isomerase deficiency: effect of F240L mutation on enzyme structure
Analyse Triosephosphate isomerase deficiency: effect of F240L mutation on enzyme… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UP1
- Type
- protein
- Length
- 491 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1, 4.2.3.3
- UniProt
- P60174
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triosephosphate isomerase (EC 5.3.1.1, 4.2.3.3) | protein | 245 | 45% helix, 17% strand | P60174 |
| B | Triosephosphate isomerase (EC 5.3.1.1, 4.2.3.3) | protein | 246 | 45% helix, 16% strand | P60174 |
Ligands and binding sites
- IPA · Isopropyl alcohol · additive · 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 | 53 | 0.70 | 0.98 | 16 | empty |
| 2 | 141 | 0.45 | 0.76 | 29 | empty |
| 3 | 106 | 0.41 | 0.76 | 24 | empty |
| 4 | 54 | 0.37 | 0.80 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1793 Ų buried · 43 hydrogen bonds · protein-protein
Compared structures
- 6UP1 · Triosephosphate isomerase deficiency: Effect of F240L mutation on enzyme structure · the same entry in another collection · chain A against A, TM-score 1.00
- P60174 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase (P60174) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P60174
- Elsewhere: RCSB PDB 6UP1 · PDBe 6UP1 · UniProt P60174
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