1LYE

DISSECTION OF HELIX CAPPING IN T4 LYSOZYME BY STRUCTURAL AND THERMODYNAMIC ANALYSIS OF SIX AMINO ACID SUBSTITUTIONS AT THR 59

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL A 173

Chain	Residue
A	LYS124
A	THR142
A	ASN144
A	ARG145
A	HOH209
A	HOH291

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site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 178

Chain	Residue
A	LYS135
A	SER136

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site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE BME A 901

Chain	Residue
A	BME902
A	ASP72

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site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BME A 902

Chain	Residue
A	ALA93
A	ILE100
A	BME901

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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
A	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
A	ASP20

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

Chain	Residue	Details
A	LEU32
A	PHE104

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

Chain	Residue	Details
A	SER117
A	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
A	GLU11
A	ASP20

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site_id	MCSA1
Number of Residues	2
Details	M-CSA 921

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

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