Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2G4N

Anomalous substructure of alpha-lactalbumin

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	0005615	cellular_component	extracellular space
A	0005989	biological_process	lactose biosynthetic process
A	0032355	biological_process	response to estradiol
A	0032570	biological_process	response to progesterone
A	0042802	molecular_function	identical protein binding
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
A	1903494	biological_process	response to dehydroepiandrosterone
A	1903496	biological_process	response to 11-deoxycorticosterone
B	0003796	molecular_function	lysozyme activity
B	0004461	molecular_function	lactose synthase activity
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005989	biological_process	lactose biosynthetic process
B	0032355	biological_process	response to estradiol
B	0032570	biological_process	response to progesterone
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0050829	biological_process	defense response to Gram-negative bacterium
B	0050830	biological_process	defense response to Gram-positive bacterium
B	1903494	biological_process	response to dehydroepiandrosterone
B	1903496	biological_process	response to 11-deoxycorticosterone
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	0005615	cellular_component	extracellular space
C	0005989	biological_process	lactose biosynthetic process
C	0032355	biological_process	response to estradiol
C	0032570	biological_process	response to progesterone
C	0042802	molecular_function	identical protein binding
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
C	1903494	biological_process	response to dehydroepiandrosterone
C	1903496	biological_process	response to 11-deoxycorticosterone
D	0003796	molecular_function	lysozyme activity
D	0004461	molecular_function	lactose synthase activity
D	0005509	molecular_function	calcium ion binding
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0005989	biological_process	lactose biosynthetic process
D	0032355	biological_process	response to estradiol
D	0032570	biological_process	response to progesterone
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0050829	biological_process	defense response to Gram-negative bacterium
D	0050830	biological_process	defense response to Gram-positive bacterium
D	1903494	biological_process	response to dehydroepiandrosterone
D	1903496	biological_process	response to 11-deoxycorticosterone
E	0003796	molecular_function	lysozyme activity
E	0004461	molecular_function	lactose synthase activity
E	0005509	molecular_function	calcium ion binding
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005615	cellular_component	extracellular space
E	0005989	biological_process	lactose biosynthetic process
E	0032355	biological_process	response to estradiol
E	0032570	biological_process	response to progesterone
E	0042802	molecular_function	identical protein binding
E	0046872	molecular_function	metal ion binding
E	0050829	biological_process	defense response to Gram-negative bacterium
E	0050830	biological_process	defense response to Gram-positive bacterium
E	1903494	biological_process	response to dehydroepiandrosterone
E	1903496	biological_process	response to 11-deoxycorticosterone
F	0003796	molecular_function	lysozyme activity
F	0004461	molecular_function	lactose synthase activity
F	0005509	molecular_function	calcium ion binding
F	0005515	molecular_function	protein binding
F	0005576	cellular_component	extracellular region
F	0005615	cellular_component	extracellular space
F	0005989	biological_process	lactose biosynthetic process
F	0032355	biological_process	response to estradiol
F	0032570	biological_process	response to progesterone
F	0042802	molecular_function	identical protein binding
F	0046872	molecular_function	metal ion binding
F	0050829	biological_process	defense response to Gram-negative bacterium
F	0050830	biological_process	defense response to Gram-positive bacterium
F	1903494	biological_process	response to dehydroepiandrosterone
F	1903496	biological_process	response to 11-deoxycorticosterone

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 201

Chain	Residue
C	LYS79
C	ASP82
C	ASP84
C	ASP87
C	ASP88
C	HOH210

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 202

Chain	Residue
D	ASP87
D	ASP88
D	HOH212
D	LYS79
D	ASP82
D	ASP84

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 203

Chain	Residue
A	LYS79
A	ASP82
A	ASP84
A	ASP87
A	ASP88

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 204

Chain	Residue
B	LYS79
B	ASP82
B	ASP84
B	ASP87
B	ASP88

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA F 205

Chain	Residue
F	LYS79
F	ASP82
F	ASP84
F	ASP87
F	ASP88
F	HOH211
F	HOH212

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 206

Chain	Residue
E	LYS79
E	ASP82
E	ASP84
E	ASP87
E	ASP88
E	HOH212

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K B 207

Chain	Residue
B	GLN2
B	GLN2
B	GLY35
B	GLY35

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K A 208

Chain	Residue
A	GLN2
A	GLN2
A	GLY35
A	GLY35

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS73-CYS91

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8805552","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HFZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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