ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Amyloid-beta precursor protein

Intermolecular
Cysteine 144 and cysteine 133
Cysteine 38 and cysteine 38
Cysteine 105 and cysteine 105
Cysteine 291 and cysteine 337
Cysteine 144 and cysteine 187
Cysteine 291 and cysteine 316
Cysteine 174 and cysteine 133
Cysteine 174 and cysteine 187
Cysteine 63 of Kallikrein-6 and cysteine 300
Cysteine 432 of Coagulation factor XI and cysteine 300
More...
Cysteine 68 of PRSS3 protein and cysteine 300
Cysteine 121 of Trypsin-3 and cysteine 300
Cysteine 98 and cysteine 98
Cysteine 416 of Coagulation factor XI and cysteine 300
Cysteine 105 of Trypsin-3 and cysteine 300
Cysteine 68 of PRSS3 protein and cysteine 324
Cysteine 121 of Trypsin-3 and cysteine 324
Cysteine 52 of PRSS3 protein and cysteine 300
Cysteine 47 of Kallikrein-6 and cysteine 300
Cysteine 38 and cysteine 5
Intramolecular
Cysteine 291 and cysteine 341
Cysteine 316 and cysteine 337
Cysteine 133 and cysteine 187
Cysteine 158 and cysteine 186
Cysteine 144 and cysteine 174
Cysteine 38 and cysteine 62
Cysteine 73 and cysteine 117
Cysteine 98 and cysteine 105
Cysteine 300 and cysteine 324
Cysteine 337 and cysteine 341
Cysteine 316 and cysteine 341
Cysteine 186 and cysteine 187
Cysteine 158 and cysteine 187
Cysteine 133 and cysteine 186
Cysteine 133 and cysteine 158
Cysteine 324 and cysteine 14
Cysteine 8 and cysteine 316
A redox-regulated disulphide may form between two units of Amyloid-beta precursor protein at cysteines 144 and 133.

Details

Redox score ?
64
PDB code
2fk3
Structure name
structure of the alzheimer's amyloid precursor protein (app) copper binding domain in 'large unit cell' form
Structure deposition date
2006-01-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide A name
Amyloid-beta precursor protein
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
P05067
Peptide B accession
P05067
Peptide A residue number
144
Peptide B residue number
133

Ligandability

Cysteine 144 of Amyloid-beta precursor protein

Cysteine 133 of Amyloid-beta precursor protein

A redox-regulated disulphide may form between two units of Amyloid-beta precursor protein at cysteines 38 and 38 (21 and 21 respectively in this structure).

Details

Redox score ?
62
PDB code
7rtz
Structure name
x-ray crystallographic structure of a beta-hairpin peptide derived from amyloid beta 14-40
Structure deposition date
2021-08-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide A name
Amyloid-beta precursor protein
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
P05067
Peptide B accession
P05067
Peptide A residue number
38
Peptide B residue number
38

Ligandability

A redox-regulated disulphide may form between two units of Amyloid-beta precursor protein at cysteines 105 and 105. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
3ktm
Structure name
structure of the heparin-induced e1-dimer of the amyloid precursor protein (app)
Structure deposition date
2009-11-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide A name
Amyloid-beta precursor protein
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
P05067
Peptide B accession
P05067
Peptide A residue number
105
Peptide B residue number
105

Ligandability

A redox-regulated disulphide may form between two units of Amyloid-beta precursor protein at cysteines 291 and 337 (5 and 51 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
5nx3
Structure name
combinatorial engineering of proteolytically resistant appi variants that selectively inhibit human kallikrein 6 for cancer therapy
Structure deposition date
2017-05-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide A name
Amyloid-beta precursor protein
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
P05067
Peptide B accession
P05067
Peptide A residue number
291
Peptide B residue number
337

Ligandability

Cysteine 291 of Amyloid-beta precursor protein

Cysteine 337 of Amyloid-beta precursor protein

A redox-regulated disulphide may form between two units of Amyloid-beta precursor protein at cysteines 144 and 187. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
2fk3
Structure name
structure of the alzheimer's amyloid precursor protein (app) copper binding domain in 'large unit cell' form
Structure deposition date
2006-01-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide A name
Amyloid-beta precursor protein
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
P05067
Peptide B accession
P05067
Peptide A residue number
144
Peptide B residue number
187

Ligandability

Cysteine 144 of Amyloid-beta precursor protein

Cysteine 187 of Amyloid-beta precursor protein

A redox-regulated disulphide may form between two units of Amyloid-beta precursor protein at cysteines 291 and 316 (5 and 30 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
5nx1
Structure name
combinatorial engineering of proteolytically resistant appi variants that selectively inhibit human kallikrein 6 for cancer therapy
Structure deposition date
2017-05-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide A name
Amyloid-beta precursor protein
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
P05067
Peptide B accession
P05067
Peptide A residue number
291
Peptide B residue number
316

Ligandability

Cysteine 291 of Amyloid-beta precursor protein

Cysteine 316 of Amyloid-beta precursor protein

A redox-regulated disulphide may form between two units of Amyloid-beta precursor protein at cysteines 174 and 133. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
2fk3
Structure name
structure of the alzheimer's amyloid precursor protein (app) copper binding domain in 'large unit cell' form
Structure deposition date
2006-01-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide A name
Amyloid-beta precursor protein
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
P05067
Peptide B accession
P05067
Peptide A residue number
174
Peptide B residue number
133

Ligandability

Cysteine 174 of Amyloid-beta precursor protein

Cysteine 133 of Amyloid-beta precursor protein

A redox-regulated disulphide may form between two units of Amyloid-beta precursor protein at cysteines 174 and 187. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2fk3
Structure name
structure of the alzheimer's amyloid precursor protein (app) copper binding domain in 'large unit cell' form
Structure deposition date
2006-01-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide A name
Amyloid-beta precursor protein
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
P05067
Peptide B accession
P05067
Peptide A residue number
174
Peptide B residue number
187

Ligandability

Cysteine 174 of Amyloid-beta precursor protein

Cysteine 187 of Amyloid-beta precursor protein

A redox-regulated disulphide may form between cysteine 63 of Kallikrein-6 and cysteine 300 of Amyloid-beta precursor protein (58 and 14 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5nx3
Structure name
combinatorial engineering of proteolytically resistant appi variants that selectively inhibit human kallikrein 6 for cancer therapy
Structure deposition date
2017-05-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
97
Minimum pKa ?
nan
% buried
nan
Peptide A name
Kallikrein-6
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
Q92876
Peptide B accession
P05067
Peptide A residue number
63
Peptide B residue number
300

Ligandability

Cysteine 63 of Kallikrein-6

Cysteine 300 of Amyloid-beta precursor protein

A redox-regulated disulphide may form between cysteine 432 of Coagulation factor XI and cysteine 300 of Amyloid-beta precursor protein (58 and 14 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1zjd
Structure name
crystal structure of the catalytic domain of coagulation factor xi in complex with kunitz protease inhibitor domain of protease nexin ii
Structure deposition date
2005-04-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
99
Minimum pKa ?
nan
% buried
nan
Peptide A name
Coagulation factor XI
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
P03951
Peptide B accession
P05067
Peptide A residue number
432
Peptide B residue number
300

Ligandability

Cysteine 432 of Coagulation factor XI

Cysteine 300 of Amyloid-beta precursor protein

A redox-regulated disulphide may form between cysteine 68 of PRSS3 protein and cysteine 300 of Amyloid-beta precursor protein (58 and 14 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6gfi
Structure name
structure of human mesotrypsin in complex with appi variant t11v/m17r/i18f/f34v
Structure deposition date
2018-04-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
94
Minimum pKa ?
nan
% buried
nan
Peptide A name
PRSS3 protein
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
Q8N2U3
Peptide B accession
P05067
Peptide A residue number
68
Peptide B residue number
300

Ligandability

Cysteine 68 of PRSS3 protein

Cysteine 300 of Amyloid-beta precursor protein

A redox-regulated disulphide may form between cysteine 121 of Trypsin-3 and cysteine 300 of Amyloid-beta precursor protein (58 and 14 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
5c67
Structure name
human mesotrypsin in complex with amyloid precursor protein inhibitor variant appi-m17g/i18f/f34v
Structure deposition date
2015-06-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide A name
Trypsin-3
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
P35030
Peptide B accession
P05067
Peptide A residue number
121
Peptide B residue number
300

Ligandability

Cysteine 121 of Trypsin-3

Cysteine 300 of Amyloid-beta precursor protein

A redox-regulated disulphide may form between two units of Amyloid-beta precursor protein at cysteines 98 and 98. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
3ktm
Structure name
structure of the heparin-induced e1-dimer of the amyloid precursor protein (app)
Structure deposition date
2009-11-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide A name
Amyloid-beta precursor protein
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
P05067
Peptide B accession
P05067
Peptide A residue number
98
Peptide B residue number
98

Ligandability

A redox-regulated disulphide may form between cysteine 416 of Coagulation factor XI and cysteine 300 of Amyloid-beta precursor protein (40 and 14 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
1zjd
Structure name
crystal structure of the catalytic domain of coagulation factor xi in complex with kunitz protease inhibitor domain of protease nexin ii
Structure deposition date
2005-04-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
99
Minimum pKa ?
nan
% buried
nan
Peptide A name
Coagulation factor XI
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
P03951
Peptide B accession
P05067
Peptide A residue number
416
Peptide B residue number
300

Ligandability

Cysteine 416 of Coagulation factor XI

Cysteine 300 of Amyloid-beta precursor protein

A redox-regulated disulphide may form between cysteine 105 of Trypsin-3 and cysteine 300 of Amyloid-beta precursor protein (42 and 14 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
3l33
Structure name
human mesotrypsin complexed with amyloid precursor protein inhibitor(appi)
Structure deposition date
2009-12-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
95
Minimum pKa ?
nan
% buried
nan
Peptide A name
Trypsin-3
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
P35030
Peptide B accession
P05067
Peptide A residue number
105
Peptide B residue number
300

Ligandability

Cysteine 105 of Trypsin-3

Cysteine 300 of Amyloid-beta precursor protein

A redox-regulated disulphide may form between cysteine 68 of PRSS3 protein and cysteine 324 of Amyloid-beta precursor protein (58 and 38 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6gfi
Structure name
structure of human mesotrypsin in complex with appi variant t11v/m17r/i18f/f34v
Structure deposition date
2018-04-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide A name
PRSS3 protein
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
Q8N2U3
Peptide B accession
P05067
Peptide A residue number
68
Peptide B residue number
324

Ligandability

Cysteine 68 of PRSS3 protein

Cysteine 324 of Amyloid-beta precursor protein

A redox-regulated disulphide may form between cysteine 121 of Trypsin-3 and cysteine 324 of Amyloid-beta precursor protein (58 and 38 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
3l33
Structure name
human mesotrypsin complexed with amyloid precursor protein inhibitor(appi)
Structure deposition date
2009-12-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide A name
Trypsin-3
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
P35030
Peptide B accession
P05067
Peptide A residue number
121
Peptide B residue number
324

Ligandability

Cysteine 121 of Trypsin-3

Cysteine 324 of Amyloid-beta precursor protein

A redox-regulated disulphide may form between cysteine 52 of PRSS3 protein and cysteine 300 of Amyloid-beta precursor protein (42 and 14 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6gfi
Structure name
structure of human mesotrypsin in complex with appi variant t11v/m17r/i18f/f34v
Structure deposition date
2018-04-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide A name
PRSS3 protein
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
Q8N2U3
Peptide B accession
P05067
Peptide A residue number
52
Peptide B residue number
300

Ligandability

Cysteine 52 of PRSS3 protein

Cysteine 300 of Amyloid-beta precursor protein

A redox-regulated disulphide may form between cysteine 47 of Kallikrein-6 and cysteine 300 of Amyloid-beta precursor protein (42 and 14 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
5nx1
Structure name
combinatorial engineering of proteolytically resistant appi variants that selectively inhibit human kallikrein 6 for cancer therapy
Structure deposition date
2017-05-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
101
Minimum pKa ?
nan
% buried
nan
Peptide A name
Kallikrein-6
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
Q92876
Peptide B accession
P05067
Peptide A residue number
47
Peptide B residue number
300

Ligandability

Cysteine 47 of Kallikrein-6

Cysteine 300 of Amyloid-beta precursor protein

A redox-regulated disulphide may form between two units of Amyloid-beta precursor protein at cysteines 38 and 5 (21 and 5 respectively in this structure).

Details

Redox score ?
nan
PDB code
7rtz
Structure name
x-ray crystallographic structure of a beta-hairpin peptide derived from amyloid beta 14-40
Structure deposition date
2021-08-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
40
Minimum pKa ?
nan
% buried
nan
Peptide A name
Amyloid-beta precursor protein
Peptide B name
Amyloid-beta precursor protein
Peptide A accession
P05067
Peptide B accession
P05067
Peptide A residue number
38
Peptide B residue number
5

Ligandability

Cysteine 38 of Amyloid-beta precursor protein

Cysteine 5 of Amyloid-beta precursor protein

Cysteine 5 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Amyloid-beta precursor protein between cysteines 291 and 341 (5 and 55 respectively in this structure).

Details

Redox score ?
88
PDB code
1ca0
Structure name
bovine chymotrypsin complexed to appi
Structure deposition date
1997-01-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05067
Residue number A
291
Residue number B
341
Peptide name
Amyloid-beta precursor protein

Ligandability

Cysteine 291 of Amyloid-beta precursor protein

Cysteine 341 of Amyloid-beta precursor protein

A redox-regulated disulphide may form within Amyloid-beta precursor protein between cysteines 316 and 337 (30 and 51 respectively in this structure).

Details

Redox score ?
88
PDB code
5nx1
Structure name
combinatorial engineering of proteolytically resistant appi variants that selectively inhibit human kallikrein 6 for cancer therapy
Structure deposition date
2017-05-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05067
Residue number A
316
Residue number B
337
Peptide name
Amyloid-beta precursor protein

Ligandability

Cysteine 316 of Amyloid-beta precursor protein

Cysteine 337 of Amyloid-beta precursor protein

A redox-regulated disulphide may form within Amyloid-beta precursor protein between cysteines 133 and 187.

Details

Redox score ?
86
PDB code
4pwq
Structure name
high-resolution crystal structure of the e1-domain of the amyloid precursor protein
Structure deposition date
2014-03-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05067
Residue number A
133
Residue number B
187
Peptide name
Amyloid-beta precursor protein

Ligandability

Cysteine 133 of Amyloid-beta precursor protein

Cysteine 187 of Amyloid-beta precursor protein

A redox-regulated disulphide may form within Amyloid-beta precursor protein between cysteines 158 and 186.

Details

Redox score ?
86
PDB code
2fk1
Structure name
structure of the alzheimer's amyloid precursor protein (app) copper binding domain in 'small unit cell' form, cu(ii)-bound
Structure deposition date
2006-01-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05067
Residue number A
158
Residue number B
186
Peptide name
Amyloid-beta precursor protein

Ligandability

Cysteine 158 of Amyloid-beta precursor protein

Cysteine 186 of Amyloid-beta precursor protein

A redox-regulated disulphide may form within Amyloid-beta precursor protein between cysteines 144 and 174.

Details

Redox score ?
85
PDB code
7mrn
Structure name
mouse cntn5 app complex
Structure deposition date
2021-05-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
P12023
Residue number A
144
Residue number B
174
Peptide name
Amyloid-beta precursor protein

Ligandability

Cysteine 144 of Amyloid-beta precursor protein

Cysteine 174 of Amyloid-beta precursor protein

A redox-regulated disulphide may form within Amyloid-beta precursor protein between cysteines 38 and 62.

Details

Redox score ?
84
PDB code
1mwp
Structure name
n-terminal domain of the amyloid precursor protein
Structure deposition date
1999-03-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05067
Residue number A
38
Residue number B
62
Peptide name
Amyloid-beta precursor protein

Ligandability

Cysteine 38 of Amyloid-beta precursor protein

Cysteine 62 of Amyloid-beta precursor protein

A redox-regulated disulphide may form within Amyloid-beta precursor protein between cysteines 73 and 117.

Details

Redox score ?
82
PDB code
4pwq
Structure name
high-resolution crystal structure of the e1-domain of the amyloid precursor protein
Structure deposition date
2014-03-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05067
Residue number A
73
Residue number B
117
Peptide name
Amyloid-beta precursor protein

Ligandability

Cysteine 73 of Amyloid-beta precursor protein

Cysteine 117 of Amyloid-beta precursor protein

A redox-regulated disulphide may form within Amyloid-beta precursor protein between cysteines 98 and 105.

Details

Redox score ?
82
PDB code
4jfn
Structure name
crystal structure of the n-terminal, growth factor-like domain of the amyloid precursor protein bound to copper
Structure deposition date
2013-02-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
12
Peptide accession
P05067
Residue number A
98
Residue number B
105
Peptide name
Amyloid-beta precursor protein

Ligandability

Cysteine 98 of Amyloid-beta precursor protein

Cysteine 105 of Amyloid-beta precursor protein

A redox-regulated disulphide may form within Amyloid-beta precursor protein between cysteines 300 and 324 (14 and 38 respectively in this structure).

Details

Redox score ?
79
PDB code
1brc
Structure name
relocating a negative charge in the binding pocket of trypsin
Structure deposition date
1992-12-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05067
Residue number A
300
Residue number B
324
Peptide name
Amyloid-beta precursor protein

Ligandability

Cysteine 300 of Amyloid-beta precursor protein

Cysteine 324 of Amyloid-beta precursor protein

A redox-regulated disulphide may form within Amyloid-beta precursor protein between cysteines 337 and 341 (51 and 55 respectively in this structure).

Details

Redox score ?
69
PDB code
5nx3
Structure name
combinatorial engineering of proteolytically resistant appi variants that selectively inhibit human kallikrein 6 for cancer therapy
Structure deposition date
2017-05-09
Thiol separation (Å)
5
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05067
Residue number A
337
Residue number B
341
Peptide name
Amyloid-beta precursor protein

Ligandability

Cysteine 337 of Amyloid-beta precursor protein

Cysteine 341 of Amyloid-beta precursor protein

A redox-regulated disulphide may form within Amyloid-beta precursor protein between cysteines 316 and 341 (30 and 55 respectively in this structure).

Details

Redox score ?
69
PDB code
3l33
Structure name
human mesotrypsin complexed with amyloid precursor protein inhibitor(appi)
Structure deposition date
2009-12-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05067
Residue number A
316
Residue number B
341
Peptide name
Amyloid-beta precursor protein

Ligandability

Cysteine 316 of Amyloid-beta precursor protein

Cysteine 341 of Amyloid-beta precursor protein

A redox-regulated disulphide may form within Amyloid-beta precursor protein between cysteines 186 and 187. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
3ktm
Structure name
structure of the heparin-induced e1-dimer of the amyloid precursor protein (app)
Structure deposition date
2009-11-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05067
Residue number A
186
Residue number B
187
Peptide name
Amyloid-beta precursor protein

Ligandability

Cysteine 186 of Amyloid-beta precursor protein

Cysteine 187 of Amyloid-beta precursor protein

A redox-regulated disulphide may form within Amyloid-beta precursor protein between cysteines 158 and 187. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
3ktm
Structure name
structure of the heparin-induced e1-dimer of the amyloid precursor protein (app)
Structure deposition date
2009-11-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05067
Residue number A
158
Residue number B
187
Peptide name
Amyloid-beta precursor protein

Ligandability

Cysteine 158 of Amyloid-beta precursor protein

Cysteine 187 of Amyloid-beta precursor protein

A redox-regulated disulphide may form within Amyloid-beta precursor protein between cysteines 133 and 186. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
2fkl
Structure name
structure of the alzheimer's amyloid precursor protein (app) copper binding domain (residues 126- 189 of app)
Structure deposition date
2006-01-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05067
Residue number A
133
Residue number B
186
Peptide name
Amyloid-beta precursor protein

Ligandability

Cysteine 133 of Amyloid-beta precursor protein

Cysteine 186 of Amyloid-beta precursor protein

A redox-regulated disulphide may form within Amyloid-beta precursor protein between cysteines 133 and 158. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3ktm
Structure name
structure of the heparin-induced e1-dimer of the amyloid precursor protein (app)
Structure deposition date
2009-11-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05067
Residue number A
133
Residue number B
158
Peptide name
Amyloid-beta precursor protein

Ligandability

Cysteine 133 of Amyloid-beta precursor protein

Cysteine 158 of Amyloid-beta precursor protein

A redox-regulated disulphide may form within Amyloid-beta precursor protein between cysteines 324 and 14 (9 and 14 respectively in this structure).

Details

Redox score ?
nan
PDB code
5hox
Structure name
x-ray crystallographic structure of an a-beta 17_36 beta-hairpin
Structure deposition date
2016-01-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
29
Minimum pKa ?
9
% buried
0
Peptide accession
P05067
Residue number A
324
Residue number B
14
Peptide name
Amyloid-beta precursor protein

Ligandability

Cysteine 324 of Amyloid-beta precursor protein

Cysteine 14 of Amyloid-beta precursor protein

Cysteine 14 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Amyloid-beta precursor protein between cysteines 8 and 316 (8 and 18 respectively in this structure).

Details

Redox score ?
nan
PDB code
6wxm
Structure name
x-ray crystallographic structure of a beta-hairpin peptide derived from amyloid beta 16-36
Structure deposition date
2020-05-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05067
Residue number A
8
Residue number B
316
Peptide name
Amyloid-beta precursor protein

Ligandability

Cysteine 8 of Amyloid-beta precursor protein

Cysteine 316 of Amyloid-beta precursor protein

Cysteine 8 in protein A could not be asigned to a Uniprot residue.
Uncertain whether structure cysteine 18 has been assigned to correct residue.
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