Function and Biology Details
Reaction catalysed:
[Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid andN-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- P-loop containing nucleoside triphosphate hydrolase
- T4-type lysozyme
- AAA+ ATPase domain
- Dynein heavy chain AAA lid domain
- Dynein heavy chain AAA lid domain superfamily
- Dynein heavy chain region D6 P-loop domain
- Dynein heavy chain, ATP-binding dynein motor region
- Glycoside hydrolase, family 24
12 more domains
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Dynein heavy chain, cytoplasmic, Endolysin (preferred)
PDBe Complex ID:
PDB-CPX-132981 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dynein heavy chain, cytoplasmic; Endolysin
Molecule details ›
Chain: A
Length: 2661 amino acids
Theoretical weight: 304.89 KDa
Source organisms: Expression system: Saccharomyces cerevisiae
UniProt:
Sequence domains:
Length: 2661 amino acids
Theoretical weight: 304.89 KDa
Source organisms: Expression system: Saccharomyces cerevisiae
UniProt:
- Canonical:
P36022 (Residues: 1364-3038, 3064-3076, 3292-4092; Coverage: 61%) - Canonical: P00720 (Residues: 4-161; Coverage: 96%)
Sequence domains:
- Dynein heavy chain, N-terminal region 2
- Hydrolytic ATP binding site of dynein motor region
- DYN1, AAA+ ATPase lid domain
- P-loop containing dynein motor region
- Dynein heavy chain, ATPase lid domain
- P-loop containing dynein motor region D4
- Microtubule-binding stalk of dynein motor
- Phage lysozyme
- ATP-binding dynein motor region
- Dynein heavy chain region D6 P-loop domain
- Dynein heavy chain AAA lid domain
