5N47

Structure of Anticalin N7E in complex with the three-domain fragment Fn7B8 of human oncofetal fibronectin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0006826	biological_process	iron ion transport
A	0006915	biological_process	apoptotic process
A	0015891	biological_process	siderophore transport
A	0031410	cellular_component	cytoplasmic vesicle
A	0035580	cellular_component	specific granule lumen
A	0036094	molecular_function	small molecule binding
A	0042742	biological_process	defense response to bacterium
A	0042802	molecular_function	identical protein binding
A	0045087	biological_process	innate immune response
A	0060205	cellular_component	cytoplasmic vesicle lumen
A	0070062	cellular_component	extracellular exosome
A	0120162	biological_process	positive regulation of cold-induced thermogenesis
A	0140315	molecular_function	iron ion sequestering activity
A	1903981	molecular_function	enterobactin binding
C	0005506	molecular_function	iron ion binding
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0006826	biological_process	iron ion transport
C	0006915	biological_process	apoptotic process
C	0015891	biological_process	siderophore transport
C	0031410	cellular_component	cytoplasmic vesicle
C	0035580	cellular_component	specific granule lumen
C	0036094	molecular_function	small molecule binding
C	0042742	biological_process	defense response to bacterium
C	0042802	molecular_function	identical protein binding
C	0045087	biological_process	innate immune response
C	0060205	cellular_component	cytoplasmic vesicle lumen
C	0070062	cellular_component	extracellular exosome
C	0120162	biological_process	positive regulation of cold-induced thermogenesis
C	0140315	molecular_function	iron ion sequestering activity
C	1903981	molecular_function	enterobactin binding
E	0005506	molecular_function	iron ion binding
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005615	cellular_component	extracellular space
E	0006826	biological_process	iron ion transport
E	0006915	biological_process	apoptotic process
E	0015891	biological_process	siderophore transport
E	0031410	cellular_component	cytoplasmic vesicle
E	0035580	cellular_component	specific granule lumen
E	0036094	molecular_function	small molecule binding
E	0042742	biological_process	defense response to bacterium
E	0042802	molecular_function	identical protein binding
E	0045087	biological_process	innate immune response
E	0060205	cellular_component	cytoplasmic vesicle lumen
E	0070062	cellular_component	extracellular exosome
E	0120162	biological_process	positive regulation of cold-induced thermogenesis
E	0140315	molecular_function	iron ion sequestering activity
E	1903981	molecular_function	enterobactin binding

Functional Information from PROSITE/UniProt

site_id	PS00213
Number of Residues	14
Details	LIPOCALIN Lipocalin signature. NFQdnQFHGKWYVV

Chain	Residue	Details
A	ASN21-VAL34

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16037490, ECO:0000269|PubMed:16335952

Chain	Residue	Details
B	ASN1244
D	ASN1244
F	ASN1244

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0007744|PDB:3CMP

Chain	Residue	Details
A	PHE106
A	PHE134
C	PHE106
C	PHE134
E	PHE106
E	PHE134

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site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:15642259, ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U

Chain	Residue	Details
A	THR125
A	TYR138
C	THR125
C	TYR138
E	THR125
E	TYR138

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site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:7683678

Chain	Residue	Details
A	GLN1
C	GLN1
E	GLN1

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site_id	SWS_FT_FI5
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10684642, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:7683678, ECO:0007744|PDB:1DFV, ECO:0007744|PDB:1QQS

Chain	Residue	Details
A	ASN65
C	ASN65
E	ASN65

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