Research workbench
The functional role of the conserved active site proline of triosephosphate isomerase
Analyse The functional role of the conserved active site proline of triosephosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2J27
- Type
- protein
- Length
- 498 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
- P04789
- Ligands
- PGA, SO4
- Pockets
- 4 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Triosephosphate isomerase glycosomal (EC 5.3.1.1) | protein | 249 | 46% helix, 17% strand | P04789 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.46 | 0.85 | 17 | PGA |
| 2 | 143 | 0.43 | 0.75 | 28 | empty |
| 3 | 69 | 0.42 | 0.81 | 24 | PGA |
| 4 | 50 | 0.26 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1554 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 2J27 · The functional role of the conserved active site proline of triosephosphate isomerase. · the same entry in another collection · chain A against A, TM-score 1.00
- P04789 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase, glycosomal (P04789) · a predicted model of the same protein · chain A against A, TM-score 1.00
- 4TIM · Crystallographic and molecular modeling studies on trypanosomal triosephosphate… · a predicted model of the same protein · chain A against A, TM-score 0.98
- 4TIM · Crystallographic and molecular modeling studies on trypanosomal triosephosphate… · 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 P04789
- Elsewhere: RCSB PDB 2J27 · PDBe 2J27 · UniProt P04789
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.