Research workbench
The cohesin-dockerin complex of nagj and nagh from clostridium perfringens
Analyse The cohesin-dockerin complex of nagj and nagh from clostridium perfringens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OZN
- Type
- protein
- Length
- 264 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- O-glcnacase nagj; Hyalurononglucosaminidase
- UniProt
- Q0TR53, P26831
- Ligands
- CA, CL
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | O-glcnacase nagj | protein | 133 | 0% helix, 66% strand | Q0TR53 |
| B | Hyalurononglucosaminidase | protein | 131 | 56% helix, 2% strand | P26831 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 841 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 2OZN · The Cohesin-Dockerin Complex of NagJ and NagH from Clostridium perfringens · the same entry in another collection · chain A against A, TM-score 1.00
- Q0TR53 · AlphaFold monomer V2.0 prediction for O-glcnacase nagj (Q0TR53) · a predicted model of the same protein · chain A against A, TM-score 0.99
- P26831 · AlphaFold monomer V2.0 prediction for hyaluronoglucosaminidase (P26831) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q0TR53
- Every structure of UniProt P26831
- Elsewhere: RCSB PDB 2OZN · PDBe 2OZN · UniProt Q0TR53 · UniProt P26831
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