Research workbench
A dehydrated form of glucose isomerase collected at 100K.
Analyse A dehydrated form of glucose isomerase collected at 100K. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZBC
- Type
- protein
- Length
- 774 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Streptomyces rubiginosus
- Molecule
- Xylose isomerase
- EC
- 5.3.1.5
- UniProt
- P24300
- Ligands
- GLC, FRU, MN
- Pockets
- 7 · best druggability 0.72
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 49% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Xylose isomerase (EC 5.3.1.5) | protein | 387 | 49% helix, 11% strand | P24300 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A, B
- FRU · beta-D-fructofuranose · sugar · 4 copies · chains A, B
- MN · Manganese (II) ion · metal · 11 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 55 | 0.72 | 0.99 | 24 | MN |
| 2 | 545 | 0.69 | 0.78 | 48 | GLC, FRU |
| 3 | 545 | 0.67 | 0.78 | 48 | GLC, FRU |
| 4 | 227 | 0.58 | 0.80 | 36 | MN |
| 5 | 226 | 0.58 | 0.80 | 39 | empty |
Interfaces
1 interface between chains.
- A–B · 4825 Ų buried · 82 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 P24300
- Elsewhere: RCSB PDB 4ZBC · PDBe 4ZBC · UniProt P24300
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