Research workbench
Cohesin and fibronectin type-III double module construct from the clostridium perfringens glycoside hydrolase GH84C
Analyse Cohesin and fibronectin type-III double module construct from the clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2W1N
- Type
- protein
- Length
- 228 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- O-glcnacase nagj
- EC
- 3.2.1.52
- UniProt
- Q8XL08
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 61% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | O-glcnacase nagj (EC 3.2.1.52) | protein | 228 | 0% helix, 61% strand | Q8XL08 |
Ligands and binding sites
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2W1N · cohesin and fibronectin type-III double module construct from the Clostridium perfringens… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8XL08 · AlphaFold monomer V2.0 prediction for O-glcnacase nagj (Q8XL08) · a predicted model of the same protein · chain A against A, TM-score 0.74
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 Q8XL08
- Elsewhere: RCSB PDB 2W1N · PDBe 2W1N · UniProt Q8XL08
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