Research workbench
Structural characterization of difunctional glucanase-xylanse CELM2
Analyse Structural characterization of difunctional glucanase-xylanse CELM2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3II1
- Type
- protein
- Length
- 522 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A1E9A6
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 522 | — | A1E9A6 |
Compared structures
- 3II1 · Structural characterization of difunctional glucanase-xylanse CelM2 · 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 A1E9A6
- Elsewhere: RCSB PDB 3II1 · PDBe 3II1 · UniProt A1E9A6
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