Research workbench
The structure of a modular endo-beta-1,4-mannanase from Cellulomonas fimi explains the product specificity of glycoside hydrolase family 26 mannanases.
Analyse The structure of a modular endo-beta-1,4-mannanase from Cellulomonas fimi… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BVT
- Type
- protein
- Length
- 902 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.9
- Source
- CELLULOMONAS FIMI
- UniProt
- Q9XCV5
Structure
x-ray diffraction · resolution 2.9 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 451 | — | Q9XCV5 |
Compared structures
- 2BVT · The structure of a modular endo-beta-1,4-mannanase from cellulomonas fimi explains the… · 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 Q9XCV5
- Elsewhere: RCSB PDB 2BVT · PDBe 2BVT · UniProt Q9XCV5
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