148L

A COVALENT ENZYME-SUBSTRATE INTERMEDIATE WITH SACCHARIDE DISTORTION IN A MUTANT T4 LYSOZYME

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0003796	molecular_function	lysozyme activity
E	0009253	biological_process	peptidoglycan catabolic process
E	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
E	0016998	biological_process	cell wall macromolecule catabolic process
E	0030430	cellular_component	host cell cytoplasm
E	0031640	biological_process	killing of cells of another organism
E	0042742	biological_process	defense response to bacterium
E	0044659	biological_process	viral release from host cell by cytolysis

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098

Chain	Residue	Details
E	GLU11

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098

Chain	Residue	Details
E	ASP20

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:8266098

Chain	Residue	Details
E	LEU32
E	PHE104

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site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000303|PubMed:7831309

Chain	Residue	Details
E	SER117
E	ASN132

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 206l

Chain	Residue	Details
E	GLU11
E	ASP20

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site_id	MCSA1
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
E	GLU11	proton shuttle (general acid/base)
E	ASP20	covalent catalysis

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