Research workbench
Transaldolase wt of thermoplasma acidophilum
Analyse Transaldolase wt of thermoplasma acidophilum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3S0C
- Type
- protein
- Length
- 1,108 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable transaldolase
- EC
- 2.2.1.2
- UniProt
- Q9HKI3
- Pockets
- 7 · best druggability 0.60
Structure
x-ray diffraction · 3 distinct chains · 51% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable transaldolase (EC 2.2.1.2) | protein | 218 | 51% helix, 17% strand | Q9HKI3 |
| B | Probable transaldolase (EC 2.2.1.2) | protein | 221 | 51% helix, 17% strand | Q9HKI3 |
| C, D, E | Probable transaldolase (EC 2.2.1.2) | protein | 223 | 52% helix, 17% strand | Q9HKI3 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 233 | 0.60 | 0.80 | 33 | empty |
| 2 | 137 | 0.54 | 0.81 | 17 | empty |
| 3 | 204 | 0.50 | 0.76 | 32 | empty |
| 4 | 102 | 0.40 | 0.77 | 26 | GOL |
| 5 | 98 | 0.39 | 0.76 | 23 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1895 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 1818 Ų buried · 16 hydrogen bonds · protein-protein
- D–E · 1709 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 1564 Ų buried · 10 hydrogen bonds · protein-protein
- A–E · 1538 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (additive adduct).
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 Q9HKI3
- Elsewhere: RCSB PDB 3S0C · PDBe 3S0C · UniProt Q9HKI3
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