Research workbench
Crystal structure of CELM2, a bifunctional glucanase- xylanase protein from a metagenome library
Analyse Crystal structure of CELM2, a bifunctional glucanase- xylanase protein from a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FW6
- Type
- protein
- Length
- 519 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellulase
- EC
- 3.2.1.4
- UniProt
- A1E9A6
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cellulase (EC 3.2.1.4) | protein | 519 | 32% helix, 26% strand | A1E9A6 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3FW6 · Crystal structure of CelM2, a bifunctional glucanase-xylanase protein from a metagenome… · 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 3FW6 · PDBe 3FW6 · UniProt A1E9A6
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