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Carbohydrate binding module (CBM6CM-2) from cellvibrio mixtus lichenase 5A in complex with glc-4GLC-3GLC-4GLC
Analyse Carbohydrate binding module (CBM6CM-2) from cellvibrio mixtus lichenase 5A in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UZ0
- Type
- protein
- Length
- 131 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellulase B
- UniProt
- O07653
- Ligands
- BGC, CA, CL
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cellulase B | protein | 131 | 2% helix, 58% strand | O07653 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 4 copies · chains A
- CA · Calcium ion · metal · 2 copies · chains A
- CL · Chloride ion · ion · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1UZ0 · Carbohydrate binding module (CBM6cm-2) from Cellvibrio mixtus lichenase 5A in complex… · 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 O07653
- Elsewhere: RCSB PDB 1UZ0 · PDBe 1UZ0 · UniProt O07653
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