Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3CDO

Bacteriophage T4 lysozyme mutant R96V in wildtype background at low temperature

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0003824	molecular_function	catalytic activity
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
B	0003796	molecular_function	lysozyme activity
B	0003824	molecular_function	catalytic activity
B	0009253	biological_process	peptidoglycan catabolic process
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0016998	biological_process	cell wall macromolecule catabolic process
B	0030430	cellular_component	host cell cytoplasm
B	0031640	biological_process	killing of cells of another organism
B	0042742	biological_process	defense response to bacterium
B	0044659	biological_process	viral release from host cell by cytolysis
C	0003796	molecular_function	lysozyme activity
C	0003824	molecular_function	catalytic activity
C	0009253	biological_process	peptidoglycan catabolic process
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0016998	biological_process	cell wall macromolecule catabolic process
C	0030430	cellular_component	host cell cytoplasm
C	0031640	biological_process	killing of cells of another organism
C	0042742	biological_process	defense response to bacterium
C	0044659	biological_process	viral release from host cell by cytolysis
D	0003796	molecular_function	lysozyme activity
D	0003824	molecular_function	catalytic activity
D	0009253	biological_process	peptidoglycan catabolic process
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0016998	biological_process	cell wall macromolecule catabolic process
D	0030430	cellular_component	host cell cytoplasm
D	0031640	biological_process	killing of cells of another organism
D	0042742	biological_process	defense response to bacterium
D	0044659	biological_process	viral release from host cell by cytolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 1902

Chain	Residue
A	ARG125
B	SER38
B	LEU39
B	ASN40
B	HOH2014
B	HOH2033
B	HOH2047

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 1903

Chain	Residue
B	PHE114
B	THR115
B	ASN116
B	SER117
B	HOH1955
B	SER44
B	LYS48

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 1905

Chain	Residue
B	THR142
B	PRO143
B	ASN144
B	ARG145
B	HOH2052

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 C 1906

Chain	Residue
C	SER44
C	LYS48
C	PHE114
C	THR115
C	ASN116
C	SER117
C	ASN132
C	HOH2136

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 D 1901

Chain	Residue
C	SER38
C	LEU39
C	ASN40
D	ARG125
D	HOH2136
D	HOH2146
D	HOH2160
D	HOH2170

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 1904

Chain	Residue
D	THR142
D	PRO143
D	ASN144
D	ARG145
D	HOH2128
D	HOH2133

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE HEZ A 1901

Chain	Residue
A	ASP89
A	SER90
A	LYS124
A	HOH2103

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE HEZ C 1921

Chain	Residue
C	LEU33
C	HEZ1922

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HEZ C 1922

Chain	Residue
C	LYS35
C	MET106
C	HEZ1921

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE HEZ D 1923

Chain	Residue
D	ASP89
D	LYS124

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MPD A 1911

Chain	Residue
A	ASP72
A	ARG76
A	HOH2064
B	ILE3
B	VAL75
B	TYR88
B	HOH1970

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD A 1914

Chain	Residue
A	TYR88
A	HOH1927
A	HOH2068
B	ASP72
B	ARG76

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD D 1912

Chain	Residue
C	ASP72
C	ARG76
D	TYR88
D	HOH2052
D	HOH2060

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MPD D 1913

Chain	Residue
C	TYR88
C	HOH2144
D	VAL71
D	ASP72
D	ARG76
D	HOH2186

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

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

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 206l

Chain	Residue	Details
B	GLU11
B	ASP20

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 206l

Chain	Residue	Details
C	GLU11
C	ASP20

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 206l

Chain	Residue	Details
D	GLU11
D	ASP20

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

site_id	MCSA2
Number of Residues	2
Details	M-CSA 921

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

site_id	MCSA3
Number of Residues	2
Details	M-CSA 921

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

site_id	MCSA4
Number of Residues	2
Details	M-CSA 921

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)