Research workbench
Transaldolase B E96Q F178Y from E.COLI
Analyse Transaldolase B E96Q F178Y from E.COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RZ6
- Type
- protein
- Length
- 632 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transaldolase B
- EC
- 2.2.1.2
- UniProt
- P0A870
- Ligands
- SO4, CL
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Transaldolase B (EC 2.2.1.2) | protein | 316 | 57% helix, 13% strand | P0A870 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
- CL · Chloride ion · ion · 4 copies · chains A, B
- P6G · Hexaethylene glycol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 180 | 0.83 | 0.97 | 28 | P6G, CL |
| 2 | 109 | 0.43 | 0.77 | 24 | SO4 |
| 3 | 90 | 0.40 | 0.77 | 20 | SO4 |
Interfaces
1 interface between chains.
- A–B · 839 Ų buried · 5 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 P0A870
- Elsewhere: RCSB PDB 4RZ6 · PDBe 4RZ6 · UniProt P0A870
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