Research workbench
X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis
Analyse X-ray crystallographic structures of D-xylose isomerase-substrate complexes… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XYB
- Type
- protein
- Length
- 772 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Xylose isomerase
- EC
- 5.3.1.5
- UniProt
- P15587
- Ligands
- GLO, MG
- Pockets
- 10 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Xylose isomerase (EC 5.3.1.5) | protein | 386 | 51% helix, 10% strand | P15587 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 892 | 0.80 | 0.82 | 90 | GLO |
| 2 | 108 | 0.76 | 0.96 | 23 | empty |
| 3 | 58 | 0.73 | 0.99 | 24 | empty |
| 4 | 106 | 0.72 | 0.94 | 23 | empty |
| 5 | 53 | 0.71 | 0.98 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1527 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 1XYB · X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the… · the same entry in another collection · chain A against A, TM-score 1.00
- P15587 · AlphaFold monomer V2.0 prediction for xylose isomerase (P15587) · a predicted model of the same protein · 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 P15587
- Elsewhere: RCSB PDB 1XYB · PDBe 1XYB · UniProt P15587
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