ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Amyloid-beta A4 protein

Intermolecular
Cysteine 52 of PRSS3 protein and cysteine 472
Cysteine 68 of PRSS3 protein and cysteine 222
Cysteine 200 of PRSS3 protein and cysteine 34
Cysteine 224 of PRSS3 protein and cysteine 34
Cysteine 52 of PRSS3 protein and cysteine 222
Cysteine 52 of PRSS3 protein and cysteine 34
Cysteine 200 of PRSS3 protein and cysteine 472
Intramolecular
Cysteine 213 and cysteine 263
Cysteine 238 and cysteine 259
Cysteine 222 and cysteine 246
More...
Cysteine 259 and cysteine 263
Cysteine 238 and cysteine 263
Cysteine 213 and cysteine 259
Cysteine 213 and cysteine 238
Cysteine 472 and cysteine 34
A redox-regulated disulphide may form between cysteine 52 of PRSS3 protein and cysteine 472 of Amyloid-beta A4 protein (42 and 17 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
6har
Structure name
crystal structure of mesotrypsin in complex with appi-m17c/i18f/f34c
Structure deposition date
2018-08-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
97
Minimum pKa ?
nan
% buried
nan
Peptide A name
PRSS3 protein
Peptide B name
Amyloid-beta A4 protein
Peptide A accession
Q8N2U3
Peptide B accession
H7C0V9
Peptide A residue number
52
Peptide B residue number
472

Ligandability

Cysteine 52 of PRSS3 protein

Cysteine 472 of Amyloid-beta A4 protein

Uncertain whether structure cysteine 17 has been assigned to correct residue.
A redox-regulated disulphide may form between cysteine 68 of PRSS3 protein and cysteine 222 of Amyloid-beta A4 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
6har
Structure name
crystal structure of mesotrypsin in complex with appi-m17c/i18f/f34c
Structure deposition date
2018-08-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
95
Minimum pKa ?
nan
% buried
nan
Peptide A name
PRSS3 protein
Peptide B name
Amyloid-beta A4 protein
Peptide A accession
Q8N2U3
Peptide B accession
H7C0V9
Peptide A residue number
68
Peptide B residue number
222

Ligandability

Cysteine 68 of PRSS3 protein

Cysteine 222 of Amyloid-beta A4 protein

A redox-regulated disulphide may form between cysteine 200 of PRSS3 protein and cysteine 34 of Amyloid-beta A4 protein (191 and 34 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6har
Structure name
crystal structure of mesotrypsin in complex with appi-m17c/i18f/f34c
Structure deposition date
2018-08-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
100
Minimum pKa ?
nan
% buried
nan
Peptide A name
PRSS3 protein
Peptide B name
Amyloid-beta A4 protein
Peptide A accession
Q8N2U3
Peptide B accession
H7C0V9
Peptide A residue number
200
Peptide B residue number
34

Ligandability

Cysteine 200 of PRSS3 protein

Cysteine 34 of Amyloid-beta A4 protein

Cysteine 34 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form between cysteine 224 of PRSS3 protein and cysteine 34 of Amyloid-beta A4 protein (220 and 34 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
6har
Structure name
crystal structure of mesotrypsin in complex with appi-m17c/i18f/f34c
Structure deposition date
2018-08-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide A name
PRSS3 protein
Peptide B name
Amyloid-beta A4 protein
Peptide A accession
Q8N2U3
Peptide B accession
H7C0V9
Peptide A residue number
224
Peptide B residue number
34

Ligandability

Cysteine 224 of PRSS3 protein

Cysteine 34 of Amyloid-beta A4 protein

Cysteine 34 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form between cysteine 52 of PRSS3 protein and cysteine 222 of Amyloid-beta A4 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
6har
Structure name
crystal structure of mesotrypsin in complex with appi-m17c/i18f/f34c
Structure deposition date
2018-08-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
100
Minimum pKa ?
nan
% buried
nan
Peptide A name
PRSS3 protein
Peptide B name
Amyloid-beta A4 protein
Peptide A accession
Q8N2U3
Peptide B accession
H7C0V9
Peptide A residue number
52
Peptide B residue number
222

Ligandability

Cysteine 52 of PRSS3 protein

Cysteine 222 of Amyloid-beta A4 protein

A redox-regulated disulphide may form between cysteine 52 of PRSS3 protein and cysteine 34 of Amyloid-beta A4 protein (42 and 34 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
6har
Structure name
crystal structure of mesotrypsin in complex with appi-m17c/i18f/f34c
Structure deposition date
2018-08-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
94
Minimum pKa ?
nan
% buried
nan
Peptide A name
PRSS3 protein
Peptide B name
Amyloid-beta A4 protein
Peptide A accession
Q8N2U3
Peptide B accession
H7C0V9
Peptide A residue number
52
Peptide B residue number
34

Ligandability

Cysteine 52 of PRSS3 protein

Cysteine 34 of Amyloid-beta A4 protein

Cysteine 34 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form between cysteine 200 of PRSS3 protein and cysteine 472 of Amyloid-beta A4 protein (191 and 17 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
6har
Structure name
crystal structure of mesotrypsin in complex with appi-m17c/i18f/f34c
Structure deposition date
2018-08-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
103
Minimum pKa ?
nan
% buried
nan
Peptide A name
PRSS3 protein
Peptide B name
Amyloid-beta A4 protein
Peptide A accession
Q8N2U3
Peptide B accession
H7C0V9
Peptide A residue number
200
Peptide B residue number
472

Ligandability

Cysteine 200 of PRSS3 protein

Cysteine 472 of Amyloid-beta A4 protein

Uncertain whether structure cysteine 17 has been assigned to correct residue.
A redox-regulated disulphide may form within Amyloid-beta A4 protein between cysteines 213 and 263 (5 and 55 respectively in this structure).

Details

Redox score ?
88
PDB code
6har
Structure name
crystal structure of mesotrypsin in complex with appi-m17c/i18f/f34c
Structure deposition date
2018-08-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
H7C0V9
Residue number A
213
Residue number B
263
Peptide name
Amyloid-beta A4 protein

Ligandability

Cysteine 213 of Amyloid-beta A4 protein

Cysteine 263 of Amyloid-beta A4 protein

A redox-regulated disulphide may form within Amyloid-beta A4 protein between cysteines 238 and 259 (30 and 51 respectively in this structure).

Details

Redox score ?
87
PDB code
6har
Structure name
crystal structure of mesotrypsin in complex with appi-m17c/i18f/f34c
Structure deposition date
2018-08-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
H7C0V9
Residue number A
238
Residue number B
259
Peptide name
Amyloid-beta A4 protein

Ligandability

Cysteine 238 of Amyloid-beta A4 protein

Cysteine 259 of Amyloid-beta A4 protein

A redox-regulated disulphide may form within Amyloid-beta A4 protein between cysteines 222 and 246 (14 and 38 respectively in this structure).

Details

Redox score ?
78
PDB code
6har
Structure name
crystal structure of mesotrypsin in complex with appi-m17c/i18f/f34c
Structure deposition date
2018-08-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
H7C0V9
Residue number A
222
Residue number B
246
Peptide name
Amyloid-beta A4 protein

Ligandability

Cysteine 222 of Amyloid-beta A4 protein

Cysteine 246 of Amyloid-beta A4 protein

A redox-regulated disulphide may form within Amyloid-beta A4 protein between cysteines 259 and 263 (51 and 55 respectively in this structure).

Details

Redox score ?
70
PDB code
6har
Structure name
crystal structure of mesotrypsin in complex with appi-m17c/i18f/f34c
Structure deposition date
2018-08-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
H7C0V9
Residue number A
259
Residue number B
263
Peptide name
Amyloid-beta A4 protein

Ligandability

Cysteine 259 of Amyloid-beta A4 protein

Cysteine 263 of Amyloid-beta A4 protein

A redox-regulated disulphide may form within Amyloid-beta A4 protein between cysteines 238 and 263 (30 and 55 respectively in this structure).

Details

Redox score ?
65
PDB code
6har
Structure name
crystal structure of mesotrypsin in complex with appi-m17c/i18f/f34c
Structure deposition date
2018-08-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
H7C0V9
Residue number A
238
Residue number B
263
Peptide name
Amyloid-beta A4 protein

Ligandability

Cysteine 238 of Amyloid-beta A4 protein

Cysteine 263 of Amyloid-beta A4 protein

A redox-regulated disulphide may form within Amyloid-beta A4 protein between cysteines 213 and 259 (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
6har
Structure name
crystal structure of mesotrypsin in complex with appi-m17c/i18f/f34c
Structure deposition date
2018-08-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
H7C0V9
Residue number A
213
Residue number B
259
Peptide name
Amyloid-beta A4 protein

Ligandability

Cysteine 213 of Amyloid-beta A4 protein

Cysteine 259 of Amyloid-beta A4 protein

A redox-regulated disulphide may form within Amyloid-beta A4 protein between cysteines 213 and 238 (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 ?
55
PDB code
6har
Structure name
crystal structure of mesotrypsin in complex with appi-m17c/i18f/f34c
Structure deposition date
2018-08-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
H7C0V9
Residue number A
213
Residue number B
238
Peptide name
Amyloid-beta A4 protein

Ligandability

Cysteine 213 of Amyloid-beta A4 protein

Cysteine 238 of Amyloid-beta A4 protein

A redox-regulated disulphide may form within Amyloid-beta A4 protein between cysteines 472 and 34 (17 and 34 respectively in this structure).

Details

Redox score ?
nan
PDB code
6har
Structure name
crystal structure of mesotrypsin in complex with appi-m17c/i18f/f34c
Structure deposition date
2018-08-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
H7C0V9
Residue number A
472
Residue number B
34
Peptide name
Amyloid-beta A4 protein

Ligandability

Cysteine 472 of Amyloid-beta A4 protein

Cysteine 34 of Amyloid-beta A4 protein

Uncertain whether structure cysteine 17 has been assigned to correct residue.
Cysteine 34 in protein B could not be asigned to a Uniprot residue.
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