Function and Biology Details
Reaction catalysed:
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
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure analysis Details
Assemblies composition:
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 ›
Chains: A, B
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, 3292-4092; Coverage: 61%) - Canonical: P00720 (Residues: 2-161; Coverage: 98%)
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
- AAA+ 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
