MolNFT v1 · #53698 · protein
Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase
2X2G · Triosephosphate isomerase, glycosomal: “Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase”. X-ray diffraction, 1 ligand (3PG), 4 pockets (best druggability 0.81). MolNFT v1 #53698 on…
- PDB
- 2X2G
- Type
- protein
- Length
- 471 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
- 3PG
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triosephosphate isomerase, glycosomal (EC 5.3.1.1) | protein | 233 | 48% helix, 17% strand | P04789 |
| B | Triosephosphate isomerase, glycosomal (EC 5.3.1.1) | protein | 238 | 48% helix, 17% strand | P04789 |
Ligands and binding sites
- 3PG · 3-phosphoglyceric acid · ligand · chains 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1102 | 0.81 | 0.82 | 98 | empty |
| 2 | 166 | 0.52 | 0.79 | 31 | 3PG |
| 3 | 85 | 0.32 | 0.74 | 15 | empty |
| 4 | 64 | 0.29 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 660 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 2X2G · Crystallographic binding studies with an engineered monomeric variant of triosephosphate… · the same entry in another collection · chain B against B, 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
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 2X2G · PDBe 2X2G · UniProt P04789
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