1NMM

beta-1,4-galactosyltransferase mutant Cys342Thr complex with alpha-lactalbumin and GlcNAc

Replaces:  1JN8

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0004461	molecular_function	lactose synthase activity
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005989	biological_process	lactose biosynthetic process
A	0032991	cellular_component	protein-containing complex
A	0046872	molecular_function	metal ion binding
A	0050829	biological_process	defense response to Gram-negative bacterium
A	0050830	biological_process	defense response to Gram-positive bacterium
B	0005975	biological_process	carbohydrate metabolic process
B	0016757	molecular_function	glycosyltransferase activity
C	0003796	molecular_function	lysozyme activity
C	0004461	molecular_function	lactose synthase activity
C	0005509	molecular_function	calcium ion binding
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005989	biological_process	lactose biosynthetic process
C	0032991	cellular_component	protein-containing complex
C	0046872	molecular_function	metal ion binding
C	0050829	biological_process	defense response to Gram-negative bacterium
C	0050830	biological_process	defense response to Gram-positive bacterium
D	0005975	biological_process	carbohydrate metabolic process
D	0016757	molecular_function	glycosyltransferase activity

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS73-CYS91

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	244
Details	Domain: {"description":"C-type lysozyme","evidences":[{"source":"PROSITE-ProRule","id":"PRU00680","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00711","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	32
Details	Binding site: {}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1fr8

Chain	Residue	Details
B	ARG359
B	GLU317
B	ASP319

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site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1fr8

Chain	Residue	Details
D	ARG359
D	GLU317
D	ASP319

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site_id	MCSA1
Number of Residues	8
Details	M-CSA 570

Chain	Residue	Details
B	ASP252	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
B	ASP254	metal ligand
B	TRP314	electrostatic stabiliser, hydrogen bond donor
B	GLU317	electrostatic stabiliser, hydrogen bond acceptor
B	ASP318	activator, electrostatic stabiliser, proton acceptor, proton donor
B	MET344	metal ligand
B	HIS347	metal ligand
B	ARG349	electrostatic stabiliser, hydrogen bond donor

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site_id	MCSA2
Number of Residues	8
Details	M-CSA 570

Chain	Residue	Details
D	ASP252	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
D	ASP254	metal ligand
D	TRP314	electrostatic stabiliser, hydrogen bond donor
D	GLU317	electrostatic stabiliser, hydrogen bond acceptor
D	ASP318	activator, electrostatic stabiliser, proton acceptor, proton donor
D	MET344	metal ligand
D	HIS347	metal ligand
D	ARG349	electrostatic stabiliser, hydrogen bond donor

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