Research workbench
Structure of CBM35 in complex with aldouronic acid
Analyse Structure of CBM35 in complex with aldouronic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QB6
- Type
- protein
- Length
- 129 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- XYN30D
- EC
- 3.2.1.8
- UniProt
- H6WCZ0
- Ligands
- XYP, GCU, CA
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 64% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | XYN30D (EC 3.2.1.8) | protein | 129 | 0% helix, 64% strand | H6WCZ0 |
Ligands and binding sites
- XYP · beta-D-xylopyranose · sugar
- GCU · alpha-D-glucopyranuronic acid · sugar · chains A
- CA · Calcium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4QB6 · Structure of CBM35 in complex with aldouronic acid · 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 H6WCZ0
- Elsewhere: RCSB PDB 4QB6 · PDBe 4QB6 · UniProt H6WCZ0
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