Research workbench
1.65 ångström resolution crystal structure of transaldolase B (tala) from francisella tularensis in covalent complex with sedoheptulose-7- phosphate
Analyse 1.65 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
- 3TNO
- 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
- I22, CL
- Pockets
- 5 · best druggability 0.86
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 | 57% helix, 12% strand | Q5NFX0 |
Ligands and binding sites
- I22 · D-altro-hept-2-ulose 7-phosphate · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 234 | 0.86 | 0.98 | 28 | empty |
| 2 | 66 | 0.72 | 0.97 | 21 | empty |
| 3 | 62 | 0.70 | 0.97 | 18 | empty |
| 4 | 127 | 0.47 | 0.78 | 22 | I22 |
| 5 | 131 | 0.46 | 0.77 | 30 | I22 |
Interfaces
1 interface between chains.
- A–B · 840 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 3TNO · 1.65 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 3TNO · PDBe 3TNO · UniProt Q5NFX0
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