Research workbench
Crystal structure of recombinant human triosephosphate isomerase at 2.8 ångströms resolution. triosephosphate isomerase related human genetic disorders and comparison with the trypanosomal enzyme
Analyse Crystal structure of recombinant human triosephosphate isomerase at 2.8… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HTI
- Type
- protein
- Length
- 496 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- P60174
- Ligands
- PGA
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Triosephosphate isomerase (EC 5.3.1.1) | protein | 248 | 42% helix, 16% strand | P60174 |
Ligands and binding sites
- PGA · 2-phosphoglycolic acid · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 137 | 0.62 | 0.86 | 29 | empty |
| 2 | 143 | 0.47 | 0.77 | 29 | empty |
| 3 | 66 | 0.40 | 0.80 | 21 | PGA |
Interfaces
1 interface between chains.
- A–B · 1761 Ų buried · 40 hydrogen bonds · protein-protein
Compared structures
- 1HTI · Crystal structure of recombinant human triosephosphate isomerase at 2.8 ångströms… · 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 A 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 1HTI · PDBe 1HTI · UniProt P60174
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