Het-PDB Navi2 (PDB: 112L)

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Ligands
Code	Name		Style	Show	Link
BME	Beta-mercaptoethanol				PoSSuM
CL	Chloride ion				PoSSuM

Non-standard Residues
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Glycosylation
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Download interaction data: 112L

Code :

112L PDBj RCSB PDB PDBe

Header :

HYDROLASE(O-GLYCOSYL)

Title :

STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME

Release Data :

1993-10-31

Compound :

mol_id	molecule	chains
1	T4 LYSOZYME	A
	ec: 3.2.1.17

Source :

mol_id	organism_scientific
1	Enterobacteria phage T4 (taxid:10665)
	expression_system_vector_type: PLASMID expression_system_plasmid: M13

Authors :

Blaber, M., Matthews, B.W.

Keywords :

HYDROLASE(O-GLYCOSYL)

Exp. method :

X-RAY DIFFRACTION ( 1.80 Å )

Citation :

Structural basis of amino acid alpha helix propensity.

Blaber, M.,Zhang, X.J.,Matthews, B.W.
(1993) Science 260 : 1637 - 1640

PubMed: 8503008

Control of Enzyme Activity by an Engineered Disulfide Bond

Matsumura, M.,Matthews, B.W.
(1989) Science 243 : 792

Structure of Bacteriophage T4 Lysozyme Refined at 1.7 Angstroms Resolution

Weaver, L.H.,Matthews, B.W.
(1987) J.Mol.Biol. 193 : 189

Chain :

UniProt :

P00720 (ENLYS_BPT4)

Reaction:	EC:	Evidence:
Reaction:	Physiological Direction:	Evidence:
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.	3.2.1.17	HAMAP-Rule:MF_04110, PubMed:4865643
	-	HAMAP-Rule:MF_04110, PubMed:4865643

PDB ID: 112L