1SF6

BINDING OF N,N',N"-TRIACETYLCHITOTRIOSE TO HEW LYSOZYME: A POWDER DIFFRACTION STUDY

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005783	cellular_component	endoplasmic reticulum
A	0016231	molecular_function	beta-N-acetylglucosaminidase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016998	biological_process	cell wall macromolecule catabolic process
A	0031640	biological_process	killing of cells of another organism
A	0042742	biological_process	defense response to bacterium
A	0042802	molecular_function	identical protein binding
A	0050829	biological_process	defense response to Gram-negative bacterium
A	0050830	biological_process	defense response to Gram-positive bacterium
A	0051672	biological_process	obsolete catabolism by organism of cell wall peptidoglycan in other organism

Functional Information from PROSITE/UniProt

site_id	PS00128
Number of Residues	19
Details	GLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CnipCsaLlssDItasvnC

Chain	Residue	Details
A	CYS76-CYS94

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE:

Chain	Residue	Details
A	GLU35
A	ASP52

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	ASP101

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 132l

Chain	Residue	Details
A	GLU35
A	ASP52

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site_id	MCSA1
Number of Residues	6
Details	M-CSA 203

Chain	Residue	Details
A	GLU35	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ASN46
A	ASP48
A	SER50
A	ASP52	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
A	ASN59

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