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Structure of CBM32-3 from a family 31 glycoside hydrolase from clostridium perfringens in complex with galactose
Analyse Structure of CBM32-3 from a family 31 glycoside hydrolase from clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LKS
- Type
- protein
- Length
- 314 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycosyl hydrolase, family 31/FIBRONECTIN type III domain protein
- UniProt
- Q0TRJ3
- Ligands
- GAL, CA
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Glycosyl hydrolase, family 31/FIBRONECTIN type III domain protein | protein | 157 | 5% helix, 48% strand | Q0TRJ3 |
Ligands and binding sites
- GAL · beta-D-galactopyranose · sugar · 2 copies · chains A, C
- CA · Calcium ion · metal · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–C · 491 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 4LKS · Structure of CBM32-3 from a family 31 glycoside hydrolase from Clostridium perfringens in… · 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 Q0TRJ3
- Elsewhere: RCSB PDB 4LKS · PDBe 4LKS · UniProt Q0TRJ3
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