Research workbench
Transketolase from escherichia COLI
Analyse Transketolase from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QGD
- Type
- protein
- Length
- 1,324 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (transketolase)
- EC
- 2.2.1.1
- UniProt
- P27302
- Ligands
- TPP, CA, SO4
- Pockets
- 13 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (transketolase) (EC 2.2.1.1) | protein | 662 | 47% helix, 14% strand | P27302 |
Ligands and binding sites
- TPP · Thiamine diphosphate · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 366 | 0.77 | 0.87 | 50 | TPP, SO4 |
| 2 | 354 | 0.76 | 0.87 | 50 | SO4, CA, TPP |
| 3 | 806 | 0.70 | 0.76 | 93 | empty |
| 4 | 211 | 0.50 | 0.76 | 29 | empty |
| 5 | 235 | 0.49 | 0.75 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 4257 Ų buried · 69 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 P27302
- Elsewhere: RCSB PDB 1QGD · PDBe 1QGD · UniProt P27302
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