CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.530 | Lysozyme |
|
1.10.530.40 |
Domain Context
CATH Clusters
| Superfamily | 1.10.530.40 |
| Functional Family |
Enzyme Information
| 3.2.1.17 |
Lysozyme.
based on mapping to UniProt P00720
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl- D-glucosamine residues in chitodextrins.
-!- Cf. EC 3.2.1.14.
|
UniProtKB Entries (1)
| P00720 |
ENLYS_BPT4
Escherichia virus T4
Endolysin
|
PDB Structure
| PDB | 1CU5 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.
Biochemistry
|
