Research workbench
Thiamine pyrophosphate bound transketolase from lactobacillus salivarius at 2.2A resolution
Analyse Thiamine pyrophosphate bound transketolase from lactobacillus salivarius at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C7X
- Type
- protein
- Length
- 662 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transketolase
- EC
- 2.2.1.1
- UniProt
- Q1WQU8
- Ligands
- TPP, MG
- Pockets
- 6 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transketolase (EC 2.2.1.1) | protein | 662 | 47% helix, 13% strand | Q1WQU8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.51 | 0.85 | 19 | TPP |
| 2 | 161 | 0.45 | 0.75 | 25 | empty |
| 3 | 129 | 0.39 | 0.74 | 23 | empty |
| 4 | 81 | 0.35 | 0.76 | 18 | empty |
| 5 | 84 | 0.34 | 0.75 | 19 | empty |
Compared structures
- 4C7X · Thiamine Pyrophosphate Bound Transketolase from Lactobacillus salivarius at 2.2A… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q1WQU8
- Elsewhere: RCSB PDB 4C7X · PDBe 4C7X · UniProt Q1WQU8
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