Research workbench
Crystal structure of xanthan lyase (N194A)
Analyse Crystal structure of xanthan lyase (N194A) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1X1H
- 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
- 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 | — |
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 | 1140 | 0.77 | 0.79 | 81 | empty |
| 2 | 146 | 0.42 | 0.74 | 33 | empty |
| 3 | 102 | 0.36 | 0.74 | 19 | empty |
Compared structures
- 1X1H · Crystal Structure of Xanthan Lyase (N194A) · 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
- Elsewhere: RCSB PDB 1X1H · PDBe 1X1H
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