Research workbench
Crystal structure of xanthan lyase (N194A) complexed with a product
Analyse Crystal structure of xanthan lyase (N194A) complexed with a product in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1X1I
- Type
- protein
- Length
- 752 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Xanthan lyase
- EC
- 4.2.2.12
- UniProt
- Q9AQS0
- Ligands
- 46M
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xanthan lyase (EC 4.2.2.12) | protein | 752 | 32% helix, 28% strand | Q9AQS0 |
Ligands and binding sites
- 46M · (4ar,6r,7s,8r,8as)-hexahydro-6,7,8-trihydroxy-2-methylpyrano[3,2-d][1,3]dioxine-2-carboxylic acid · ligand · chains A
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 | 1144 | 0.77 | 0.79 | 84 | 46M |
| 2 | 134 | 0.42 | 0.75 | 29 | empty |
| 3 | 108 | 0.37 | 0.75 | 19 | empty |
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 Q9AQS0
- Elsewhere: RCSB PDB 1X1I · PDBe 1X1I · UniProt Q9AQS0
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