Research workbench
Structural and biochemical characterization of a novel carbohydrate binding module of endoglucanase CEL5A from eubacterium cellulosolvens
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
- 4AEM
- Type
- protein
- Length
- 126 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoglucanase CEL5A
- UniProt
- Q3LHN3
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoglucanase CEL5A | protein | 126 | 9% helix, 48% strand | Q3LHN3 |
Compared structures
- 4AEM · 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 4AEM · PDBe 4AEM · UniProt Q3LHN3
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