1L89

SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0003824	molecular_function	catalytic activity
A	0008152	biological_process	metabolic process
A	0009253	biological_process	peptidoglycan catabolic process
A	0016787	molecular_function	hydrolase activity
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	5
Details	BINDING SITE FOR RESIDUE CL A 173

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

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 178

Chain	Residue
A	LYS135
A	HOH215
A	HOH246

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

Chain	Residue
A	BME902
A	VAL75

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site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE BME A 902

Chain	Residue
A	ALA93
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	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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