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Crystal structure of mouse transaldolase
Analyse Crystal structure of mouse transaldolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2E1D
- Type
- protein
- Length
- 642 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transaldolase
- EC
- 2.2.1.2
- UniProt
- Q93092
- Ligands
- SO3
- Pockets
- 5 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 59% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transaldolase (EC 2.2.1.2) | protein | 321 | 58% helix, 12% strand | Q93092 |
| B | Transaldolase (EC 2.2.1.2) | protein | 321 | 60% helix, 12% strand | Q93092 |
Ligands and binding sites
- SO3 · Sulfite ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 209 | 0.85 | 0.98 | 25 | empty |
| 2 | 132 | 0.47 | 0.78 | 26 | SO3 |
| 3 | 121 | 0.46 | 0.78 | 26 | SO3 |
| 4 | 71 | 0.31 | 0.74 | 16 | empty |
| 5 | 52 | 0.28 | 0.74 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 920 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
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 Q93092
- Elsewhere: RCSB PDB 2E1D · PDBe 2E1D · UniProt Q93092
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