Research workbench
Structure of CBM32-1 from a family 31 glycoside hydrolase from clostridium perfringens
Analyse Structure of CBM32-1 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
- 4LPL
- Type
- protein
- Length
- 142 residues
- Chains
- 1
- 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
- CA, MG
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycosyl hydrolase, family 31/FIBRONECTIN type III domain protein | protein | 142 | 5% helix, 49% strand | Q0TRJ3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4LPL · Structure of CBM32-1 from a family 31 glycoside hydrolase from Clostridium perfringens · 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 4LPL · PDBe 4LPL · UniProt Q0TRJ3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.