Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4MVL

Crystal structure of an engineered lipocalin (Anticalin H1GA) in complex with the Alzheimer amyloid peptide Abeta1-40

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
B	0005506	molecular_function	iron ion binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0006826	biological_process	iron ion transport
B	0006915	biological_process	apoptotic process
B	0015891	biological_process	siderophore transport
B	0031410	cellular_component	cytoplasmic vesicle
B	0035580	cellular_component	specific granule lumen
B	0036094	molecular_function	small molecule binding
B	0042742	biological_process	defense response to bacterium
B	0042802	molecular_function	identical protein binding
B	0045087	biological_process	innate immune response
B	0060205	cellular_component	cytoplasmic vesicle lumen
B	0070062	cellular_component	extracellular exosome
B	0120162	biological_process	positive regulation of cold-induced thermogenesis
B	0140315	molecular_function	iron ion sequestering activity
B	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
D	0005506	molecular_function	iron ion binding
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0006826	biological_process	iron ion transport
D	0006915	biological_process	apoptotic process
D	0015891	biological_process	siderophore transport
D	0031410	cellular_component	cytoplasmic vesicle
D	0035580	cellular_component	specific granule lumen
D	0036094	molecular_function	small molecule binding
D	0042742	biological_process	defense response to bacterium
D	0042802	molecular_function	identical protein binding
D	0045087	biological_process	innate immune response
D	0060205	cellular_component	cytoplasmic vesicle lumen
D	0070062	cellular_component	extracellular exosome
D	0120162	biological_process	positive regulation of cold-induced thermogenesis
D	0140315	molecular_function	iron ion sequestering activity
D	1903981	molecular_function	enterobactin binding
E	0016020	cellular_component	membrane
F	0016020	cellular_component	membrane
G	0016020	cellular_component	membrane
H	0016020	cellular_component	membrane

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASN21-VAL34

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:11274207, ECO:0000269\|PubMed:26898943

Chain	Residue	Details
E	HIS6
E	HIS14
F	HIS6
F	HIS14
G	HIS6
G	HIS14
H	HIS6
H	HIS14

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305\|PubMed:10413512, ECO:0000305\|PubMed:11274207

Chain	Residue	Details
E	TYR10
F	TYR10
G	TYR10
H	TYR10
C	TRP106
C	ASN134
D	TRP106
D	ASN134

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:10413512, ECO:0000269\|PubMed:11274207, ECO:0000269\|PubMed:26898943

Chain	Residue	Details
E	HIS13
F	HIS13
G	HIS13
H	HIS13
C	GLU125
C	TYR138
D	GLU125
D	TYR138

site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Cleavage; by caspase-6; when associated with variant 670-N-L-671

Chain	Residue	Details
E	ASP1
F	ASP1
G	ASP1
H	ASP1

site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Cleavage; by ACE => ECO:0000269\|PubMed:11604391, ECO:0000269\|PubMed:16154999

Chain	Residue	Details
E	ASP7
F	ASP7
G	ASP7
H	ASP7

site_id	SWS_FT_FI6
Number of Residues	4
Details	SITE: Cleavage; by alpha-secretase => ECO:0000305\|PubMed:11851430

Chain	Residue	Details
E	LYS16
F	LYS16
G	LYS16
H	LYS16

site_id	SWS_FT_FI7
Number of Residues	4
Details	SITE: Cleavage; by theta-secretase => ECO:0000269\|PubMed:16816112

Chain	Residue	Details
E	PHE19
F	PHE19
G	PHE19
H	PHE19

site_id	SWS_FT_FI8
Number of Residues	4
Details	SITE: Implicated in free radical propagation => ECO:0000250

Chain	Residue	Details
E	GLY33
F	GLY33
G	GLY33
H	GLY33

site_id	SWS_FT_FI9
Number of Residues	4
Details	SITE: Susceptible to oxidation => ECO:0000269\|PubMed:10535332

Chain	Residue	Details
E	MET35
F	MET35
G	MET35
H	MET35

site_id	SWS_FT_FI10
Number of Residues	4
Details	SITE: Cleavage; by gamma-secretase; site 1 => ECO:0000305\|PubMed:11851430

Chain	Residue	Details
E	VAL40
F	VAL40
G	VAL40
H	VAL40

site_id	SWS_FT_FI11
Number of Residues	4
Details	CARBOHYD: O-linked (HexNAc...) tyrosine; partial => ECO:0000269\|PubMed:22576872

Chain	Residue	Details
E	TYR10
F	TYR10
G	TYR10
H	TYR10

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