Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8OTF

Ab typeII filament from Guam ALS/PDC

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004867	molecular_function	serine-type endopeptidase inhibitor activity
A	0008201	molecular_function	heparin binding
A	0016020	cellular_component	membrane
A	0046914	molecular_function	transition metal ion binding
B	0004867	molecular_function	serine-type endopeptidase inhibitor activity
B	0008201	molecular_function	heparin binding
B	0016020	cellular_component	membrane
B	0046914	molecular_function	transition metal ion binding
C	0004867	molecular_function	serine-type endopeptidase inhibitor activity
C	0008201	molecular_function	heparin binding
C	0016020	cellular_component	membrane
C	0046914	molecular_function	transition metal ion binding
D	0004867	molecular_function	serine-type endopeptidase inhibitor activity
D	0008201	molecular_function	heparin binding
D	0016020	cellular_component	membrane
D	0046914	molecular_function	transition metal ion binding
E	0004867	molecular_function	serine-type endopeptidase inhibitor activity
E	0008201	molecular_function	heparin binding
E	0016020	cellular_component	membrane
E	0046914	molecular_function	transition metal ion binding
F	0004867	molecular_function	serine-type endopeptidase inhibitor activity
F	0008201	molecular_function	heparin binding
F	0016020	cellular_component	membrane
F	0046914	molecular_function	transition metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00280
Number of Residues	19
Details	BPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FfyGGCggnrnnFdteeyC

Chain	Residue	Details
A	PHE-352-CYS-334

site_id	PS00319
Number of Residues	8
Details	APP_CUBD Amyloid precursor protein (APP) copper-binding (CuBD) domain signature. GVEFVCCP

Chain	Residue	Details
A	GLY-490-PRO-483

site_id	PS00320
Number of Residues	8
Details	APP_INTRA Amyloid precursor protein (APP) intracellular domain signature. GYENPTYK

Chain	Residue	Details
A	GLY85-LYS92

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4098
Details	TOPO_DOM: Extracellular => ECO:0000305

Chain	Residue	Details
A	LEU-653-ALA30
B	LEU-653-ALA30
C	LEU-653-ALA30
D	LEU-653-ALA30
E	LEU-653-ALA30
F	LEU-653-ALA30

site_id	SWS_FT_FI2
Number of Residues	120
Details	TRANSMEM: Helical => ECO:0000305\|PubMed:22584060, ECO:0000305\|PubMed:22654059, ECO:0000305\|PubMed:30630874

Chain	Residue	Details
A	ILE31-MET51
B	ILE31-MET51
C	ILE31-MET51
D	ILE31-MET51
E	ILE31-MET51
F	ILE31-MET51

site_id	SWS_FT_FI3
Number of Residues	282
Details	TOPO_DOM: Cytoplasmic => ECO:0000305

Chain	Residue	Details
A	LEU52-ASN99
B	LEU52-ASN99
C	LEU52-ASN99
D	LEU52-ASN99
E	LEU52-ASN99
F	LEU52-ASN99

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:8158260

Chain	Residue	Details
A	ASN-575
B	ASN-575
C	ASN-575
D	ASN-575
E	ASN-575
F	ASN-575

site_id	SWS_FT_FI5
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01217, ECO:0000269\|PubMed:17239395, ECO:0000269\|PubMed:25122912, ECO:0007744\|PDB:2FK1

Chain	Residue	Details
A	HIS-524
E	HIS-520
F	HIS-524
F	HIS-520
A	HIS-520
B	HIS-524
B	HIS-520
C	HIS-524
C	HIS-520
D	HIS-524
D	HIS-520
E	HIS-524

site_id	SWS_FT_FI6
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01217, ECO:0000269\|PubMed:17239395, ECO:0007744\|PDB:2FK1

Chain	Residue	Details
A	TYR-503
B	TYR-503
C	TYR-503
D	TYR-503
E	TYR-503
F	TYR-503

site_id	SWS_FT_FI7
Number of Residues	18
Details	BINDING: BINDING => ECO:0000305\|PubMed:8344894

Chain	Residue	Details
A	GLU-488
D	GLU-488
D	CYS-485
D	CYS-484
E	GLU-488
E	CYS-485
E	CYS-484
F	GLU-488
F	CYS-485
F	CYS-484
A	CYS-485
A	CYS-484
B	GLU-488
B	CYS-485
B	CYS-484
C	GLU-488
C	CYS-485
C	CYS-484

site_id	SWS_FT_FI8
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:11274207, ECO:0000269\|PubMed:26898943

Chain	Residue	Details
A	HIS6
E	HIS14
F	HIS6
F	HIS14
A	HIS14
B	HIS6
B	HIS14
C	HIS6
C	HIS14
D	HIS6
D	HIS14
E	HIS6

site_id	SWS_FT_FI9
Number of Residues	6
Details	BINDING: BINDING => ECO:0000305\|PubMed:10413512, ECO:0000305\|PubMed:11274207

Chain	Residue	Details
A	TYR10
B	TYR10
C	TYR10
D	TYR10
E	TYR10
F	TYR10

site_id	SWS_FT_FI10
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:10413512, ECO:0000269\|PubMed:11274207, ECO:0000269\|PubMed:26898943

Chain	Residue	Details
A	HIS13
B	HIS13
C	HIS13
D	HIS13
E	HIS13
F	HIS13

site_id	SWS_FT_FI11
Number of Residues	6
Details	SITE: Required for Cu(2+) reduction => ECO:0000255\|PROSITE-ProRule:PRU01217

Chain	Residue	Details
A	MET-501
B	MET-501
C	MET-501
D	MET-501
E	MET-501
F	MET-501

site_id	SWS_FT_FI12
Number of Residues	12
Details	SITE: Cleavage; by caspases => ECO:0000269\|PubMed:10319819

Chain	Residue	Details
A	ASP-474
E	ASP-452
F	ASP-474
F	ASP-452
A	ASP-452
B	ASP-474
B	ASP-452
C	ASP-474
C	ASP-452
D	ASP-474
D	ASP-452
E	ASP-474

site_id	SWS_FT_FI13
Number of Residues	6
Details	SITE: Reactive bond

Chain	Residue	Details
A	ARG-370
B	ARG-370
C	ARG-370
D	ARG-370
E	ARG-370
F	ARG-370

site_id	SWS_FT_FI14
Number of Residues	6
Details	SITE: Cleavage; by beta-secretase => ECO:0000305\|PubMed:11851430

Chain	Residue	Details
A	MET0
B	MET0
C	MET0
D	MET0
E	MET0
F	MET0

site_id	SWS_FT_FI15
Number of Residues	6
Details	SITE: Cleavage; by caspase-6; when associated with variant 670-N-L-671

Chain	Residue	Details
A	ASP1
B	ASP1
C	ASP1
D	ASP1
E	ASP1
F	ASP1

site_id	SWS_FT_FI16
Number of Residues	6
Details	SITE: Cleavage; by ACE => ECO:0000269\|PubMed:11604391, ECO:0000269\|PubMed:16154999

Chain	Residue	Details
A	ASP7
B	ASP7
C	ASP7
D	ASP7
E	ASP7
F	ASP7

site_id	SWS_FT_FI17
Number of Residues	6
Details	SITE: Cleavage; by alpha-secretase => ECO:0000305\|PubMed:11851430

Chain	Residue	Details
A	LYS16
B	LYS16
C	LYS16
D	LYS16
E	LYS16
F	LYS16

site_id	SWS_FT_FI18
Number of Residues	6
Details	SITE: Cleavage; by theta-secretase => ECO:0000269\|PubMed:16816112

Chain	Residue	Details
A	PHE19
B	PHE19
C	PHE19
D	PHE19
E	PHE19
F	PHE19

site_id	SWS_FT_FI19
Number of Residues	6
Details	SITE: Implicated in free radical propagation => ECO:0000250

Chain	Residue	Details
A	GLY33
B	GLY33
C	GLY33
D	GLY33
E	GLY33
F	GLY33

site_id	SWS_FT_FI20
Number of Residues	6
Details	SITE: Susceptible to oxidation => ECO:0000269\|PubMed:10535332

Chain	Residue	Details
A	MET35
B	MET35
C	MET35
D	MET35
E	MET35
F	MET35

site_id	SWS_FT_FI21
Number of Residues	6
Details	SITE: Cleavage; by gamma-secretase; site 1 => ECO:0000305\|PubMed:11851430

Chain	Residue	Details
A	VAL40
B	VAL40
C	VAL40
D	VAL40
E	VAL40
F	VAL40

site_id	SWS_FT_FI22
Number of Residues	6
Details	SITE: Cleavage; by gamma-secretase; site 2 => ECO:0000305\|PubMed:11851430

Chain	Residue	Details
A	ALA42
B	ALA42
C	ALA42
D	ALA42
E	ALA42
F	ALA42

site_id	SWS_FT_FI23
Number of Residues	6
Details	SITE: Cleavage; by gamma-secretase; site 3 => ECO:0000269\|PubMed:11851430, ECO:0000305\|PubMed:30630874

Chain	Residue	Details
A	LEU49
B	LEU49
C	LEU49
D	LEU49
E	LEU49
F	LEU49

site_id	SWS_FT_FI24
Number of Residues	6
Details	SITE: Cleavage; by caspase-6, caspase-8 or caspase-9 => ECO:0000269\|PubMed:10319819

Chain	Residue	Details
A	ASP68
B	ASP68
C	ASP68
D	ASP68
E	ASP68
F	ASP68

site_id	SWS_FT_FI25
Number of Residues	6
Details	MOD_RES: Phosphoserine; by CK2 => ECO:0000269\|PubMed:8999878

Chain	Residue	Details
A	SER-473
B	SER-473
C	SER-473
D	SER-473
E	SER-473
F	SER-473

site_id	SWS_FT_FI26
Number of Residues	6
Details	MOD_RES: Phosphoserine; by CK1 => ECO:0000269\|PubMed:8999878

Chain	Residue	Details
A	SER-465
B	SER-465
C	SER-465
D	SER-465
E	SER-465
F	SER-465

site_id	SWS_FT_FI27
Number of Residues	18
Details	MOD_RES: Sulfotyrosine => ECO:0000255

Chain	Residue	Details
A	TYR-454
D	TYR-454
D	TYR-409
D	TYR-335
E	TYR-454
E	TYR-409
E	TYR-335
F	TYR-454
F	TYR-409
F	TYR-335
A	TYR-409
A	TYR-335
B	TYR-454
B	TYR-409
B	TYR-335
C	TYR-454
C	TYR-409
C	TYR-335

site_id	SWS_FT_FI28
Number of Residues	6
Details	MOD_RES: Phosphoserine; by FAM20C => ECO:0000269\|PubMed:26091039

Chain	Residue	Details
A	SER-230
B	SER-230
C	SER-230
D	SER-230
E	SER-230
F	SER-230

site_id	SWS_FT_FI29
Number of Residues	6
Details	MOD_RES: Phosphotyrosine => ECO:0000269\|PubMed:26091039

Chain	Residue	Details
A	TYR-174
B	TYR-174
C	TYR-174
D	TYR-174
E	TYR-174
F	TYR-174

site_id	SWS_FT_FI30
Number of Residues	6
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P08592

Chain	Residue	Details
A	THR58
B	THR58
C	THR58
D	THR58
E	THR58
F	THR58

site_id	SWS_FT_FI31
Number of Residues	6
Details	MOD_RES: Phosphoserine; by APP-kinase I => ECO:0000250\|UniProtKB:P08592

Chain	Residue	Details
A	SER59
B	SER59
C	SER59
D	SER59
E	SER59
F	SER59

site_id	SWS_FT_FI32
Number of Residues	6
Details	MOD_RES: Phosphothreonine; by CDK5 and MAPK10 => ECO:0000269\|PubMed:28720718, ECO:0000269\|PubMed:8131745, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	THR72
B	THR72
C	THR72
D	THR72
E	THR72
F	THR72

site_id	SWS_FT_FI33
Number of Residues	6
Details	MOD_RES: Phosphotyrosine => ECO:0000269\|PubMed:11877420

Chain	Residue	Details
A	TYR86
B	TYR86
C	TYR86
D	TYR86
E	TYR86
F	TYR86

site_id	SWS_FT_FI34
Number of Residues	6
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952

Chain	Residue	Details
A	ASN-129
B	ASN-129
C	ASN-129
D	ASN-129
E	ASN-129
F	ASN-129

site_id	SWS_FT_FI35
Number of Residues	6
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305

Chain	Residue	Details
A	ASN-100
B	ASN-100
C	ASN-100
D	ASN-100
E	ASN-100
F	ASN-100

site_id	SWS_FT_FI36
Number of Residues	18
Details	CARBOHYD: O-linked (GalNAc...) threonine; partial => ECO:0000269\|PubMed:21712440, ECO:0000269\|PubMed:22576872

Chain	Residue	Details
A	THR-38
D	THR-38
D	THR-20
D	THR-19
E	THR-38
E	THR-20
E	THR-19
F	THR-38
F	THR-20
F	THR-19
A	THR-20
A	THR-19
B	THR-38
B	THR-20
B	THR-19
C	THR-38
C	THR-20
C	THR-19

site_id	SWS_FT_FI37
Number of Residues	6
Details	CARBOHYD: O-linked (Xyl...) (chondroitin sulfate) serine; in L-APP isoforms => ECO:0000269\|PubMed:21712440

Chain	Residue	Details
A	SER-15
B	SER-15
C	SER-15
D	SER-15
E	SER-15
F	SER-15

site_id	SWS_FT_FI38
Number of Residues	6
Details	CARBOHYD: O-linked (HexNAc...) threonine; partial => ECO:0000269\|PubMed:22576872

Chain	Residue	Details
A	THR-12
B	THR-12
C	THR-12
D	THR-12
E	THR-12
F	THR-12

site_id	SWS_FT_FI39
Number of Residues	6
Details	CARBOHYD: O-linked (GalNAc...) threonine; partial => ECO:0000269\|PubMed:22576872, ECO:0000305\|PubMed:21712440

Chain	Residue	Details
A	THR-8
B	THR-8
C	THR-8
D	THR-8
E	THR-8
F	THR-8

site_id	SWS_FT_FI40
Number of Residues	6
Details	CARBOHYD: O-linked (GalNAc...) serine; partial => ECO:0000269\|PubMed:22576872, ECO:0000305\|PubMed:21712440

Chain	Residue	Details
A	SER-4
B	SER-4
C	SER-4
D	SER-4
E	SER-4
F	SER-4

site_id	SWS_FT_FI41
Number of Residues	6
Details	CARBOHYD: O-linked (HexNAc...) tyrosine; partial => ECO:0000269\|PubMed:22576872

Chain	Residue	Details
A	TYR10
B	TYR10
C	TYR10
D	TYR10
E	TYR10
F	TYR10

site_id	SWS_FT_FI42
Number of Residues	12
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250\|UniProtKB:P08592

Chain	Residue	Details
A	LYS92
F	LYS92
B	LYS92
C	LYS92
D	LYS92
E	LYS92

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)