Research workbench
X-2 engineered mutated CBM4-2 carbohydrate binding module from a thermostable rhodothermus marinus xylanase
Analyse X-2 engineered mutated CBM4-2 carbohydrate binding module from a thermostable… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Y6J
- Type
- protein
- Length
- 167 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Xylanase
- EC
- 3.2.1.8
- UniProt
- Q6V8M0
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xylanase (EC 3.2.1.8) | protein | 167 | 4% helix, 49% strand | Q6V8M0 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2Y6J · X-2 engineered mutated CBM4-2 Carbohydrate Binding Module from a Thermostable… · 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 Q6V8M0
- Elsewhere: RCSB PDB 2Y6J · PDBe 2Y6J · UniProt Q6V8M0
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