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Structural and biochemical characterization of a novel carbohydrate binding module of endoglucanase CEL5A from eubacterium cellulosolvens with a partially bound cellotetraose moeity.
Analyse Structural and biochemical characterization of a novel carbohydrate binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AFD
- Type
- protein
- Length
- 128 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoglucanase CEL5A
- UniProt
- Q3LHN3
- Ligands
- BGC
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoglucanase CEL5A | protein | 128 | 6% helix, 46% strand | Q3LHN3 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4AFD · Structural and biochemical characterization of a novel Carbohydrate Binding Module of… · 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 Q3LHN3
- Elsewhere: RCSB PDB 4AFD · PDBe 4AFD · UniProt Q3LHN3
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