Research workbench
2.0 ångström resolution crystal structure of transaldolase B (tala) from francisella tularensis in covalent complex with fructose 6- phosphate
Analyse 2.0 ångström resolution crystal structure of transaldolase B (tala) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TK7
- Type
- protein
- Length
- 637 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transaldolase
- EC
- 2.2.1.2
- UniProt
- Q5NFX0
- Ligands
- F6R
- Pockets
- 5 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transaldolase (EC 2.2.1.2) | protein | 320 | 57% helix, 12% strand | Q5NFX0 |
| B | Transaldolase (EC 2.2.1.2) | protein | 317 | 58% helix, 12% strand | Q5NFX0 |
Ligands and binding sites
- F6R · Fructose -6-phosphate · ligand · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.85 | 0.98 | 27 | empty |
| 2 | 51 | 0.68 | 0.97 | 18 | empty |
| 3 | 165 | 0.48 | 0.77 | 36 | F6R |
| 4 | 144 | 0.47 | 0.77 | 33 | F6R |
| 5 | 60 | 0.27 | 0.73 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 837 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 3TK7 · 2.0 Angstrom Resolution Crystal Structure of Transaldolase B (TalA) from Francisella… · 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 Q5NFX0
- Elsewhere: RCSB PDB 3TK7 · PDBe 3TK7 · UniProt Q5NFX0
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