Research workbench
Cycloalternan-forming enzyme from listeria monocytogenes in complex with panose
Analyse Cycloalternan-forming enzyme from listeria monocytogenes in complex with panose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HXM
- Type
- protein
- Length
- 1,060 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-xylosidase
- EC
- 3.2.1.177
- UniProt
- A0A0R1CZZ2
- Ligands
- GLC, MG, CA, CL
- Pockets
- 8 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-xylosidase (EC 3.2.1.177) | protein | 1060 | 17% helix, 37% strand | A0A0R1CZZ2 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 6 copies · chains A
- MG · Magnesium ion · metal · 5 copies · chains A
- CA · Calcium ion · metal · chains A
- CL · Chloride ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 327 | 0.62 | 0.79 | 44 | empty |
| 2 | 156 | 0.52 | 0.79 | 22 | GLC |
| 3 | 187 | 0.47 | 0.75 | 20 | empty |
| 4 | 74 | 0.45 | 0.82 | 23 | empty |
| 5 | 135 | 0.39 | 0.74 | 25 | empty |
Modifications
Observed in the structure: 30 modified (engineered).
Compared structures
- 5HXM · Cycloalternan-forming enzyme from Listeria monocytogenes in complex with panose · 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 A0A0R1CZZ2
- Elsewhere: RCSB PDB 5HXM · PDBe 5HXM · UniProt A0A0R1CZZ2
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