Research workbench
CBM6CT from clostridium thermocellum in complex with xylopentaose
Analyse CBM6CT from clostridium thermocellum in complex with xylopentaose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UXX
- Type
- protein
- Length
- 124 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Xylanase U
- EC
- 3.2.1.8
- UniProt
- O52780
- Ligands
- XYP, CA
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 62% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Xylanase U (EC 3.2.1.8) | protein | 124 | 2% helix, 62% strand | O52780 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1UXX · CBM6ct from Clostridium thermocellum in complex with xylopentaose · the same entry in another collection · chain X against X, 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 O52780
- Elsewhere: RCSB PDB 1UXX · PDBe 1UXX · UniProt O52780
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