ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Sucrase-isomaltase, intestinal

Intramolecular
Cysteine 88 and cysteine 106
Cysteine 77 and cysteine 93
Cysteine 63 and cysteine 94
Cysteine 520 and cysteine 545
Cysteine 635 and cysteine 646
Cysteine 77 and cysteine 106
Cysteine 88 and cysteine 93
Cysteine 93 and cysteine 106
Cysteine 77 and cysteine 88
Cysteine 63 and cysteine 88
More...
Cysteine 88 and cysteine 94
Cysteine 63 and cysteine 106
Cysteine 94 and cysteine 106
Cysteine 63 and cysteine 93
Cysteine 93 and cysteine 94
Cysteine 77 and cysteine 94
A redox-regulated disulphide may form within Sucrase-isomaltase, intestinal between cysteines 88 and 106 (55 and 73 respectively in this structure).

Details

Redox score ?
85
PDB code
3lpo
Structure name
crystal structure of the n-terminal domain of sucrase-isomaltase
Structure deposition date
2010-02-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14410
Residue number A
88
Residue number B
106
Peptide name
Sucrase-isomaltase, intestinal

Ligandability

Cysteine 88 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 106 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sucrase-isomaltase, intestinal between cysteines 77 and 93 (44 and 60 respectively in this structure).

Details

Redox score ?
84
PDB code
3lpo
Structure name
crystal structure of the n-terminal domain of sucrase-isomaltase
Structure deposition date
2010-02-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14410
Residue number A
77
Residue number B
93
Peptide name
Sucrase-isomaltase, intestinal

Ligandability

Cysteine 77 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 93 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sucrase-isomaltase, intestinal between cysteines 63 and 94 (30 and 61 respectively in this structure).

Details

Redox score ?
83
PDB code
3lpo
Structure name
crystal structure of the n-terminal domain of sucrase-isomaltase
Structure deposition date
2010-02-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14410
Residue number A
63
Residue number B
94
Peptide name
Sucrase-isomaltase, intestinal

Ligandability

Cysteine 63 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 94 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sucrase-isomaltase, intestinal between cysteines 520 and 545 (487 and 512 respectively in this structure).

Details

Redox score ?
83
PDB code
3lpp
Structure name
crystal complex of n-terminal sucrase-isomaltase with kotalanol
Structure deposition date
2010-02-05
Thiol separation (Å)
3
Half-sphere exposure sum ?
74
Minimum pKa ?
8
% buried
56
Peptide accession
P14410
Residue number A
520
Residue number B
545
Peptide name
Sucrase-isomaltase, intestinal

Ligandability

Cysteine 520 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 545 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sucrase-isomaltase, intestinal between cysteines 635 and 646 (602 and 613 respectively in this structure).

Details

Redox score ?
77
PDB code
3lpo
Structure name
crystal structure of the n-terminal domain of sucrase-isomaltase
Structure deposition date
2010-02-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
95
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14410
Residue number A
635
Residue number B
646
Peptide name
Sucrase-isomaltase, intestinal

Ligandability

Cysteine 635 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 646 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sucrase-isomaltase, intestinal between cysteines 77 and 106 (44 and 73 respectively in this structure).

Details

Redox score ?
71
PDB code
3lpo
Structure name
crystal structure of the n-terminal domain of sucrase-isomaltase
Structure deposition date
2010-02-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14410
Residue number A
77
Residue number B
106
Peptide name
Sucrase-isomaltase, intestinal

Ligandability

Cysteine 77 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 106 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sucrase-isomaltase, intestinal between cysteines 88 and 93 (55 and 60 respectively in this structure).

Details

Redox score ?
69
PDB code
3lpp
Structure name
crystal complex of n-terminal sucrase-isomaltase with kotalanol
Structure deposition date
2010-02-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14410
Residue number A
88
Residue number B
93
Peptide name
Sucrase-isomaltase, intestinal

Ligandability

Cysteine 88 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 93 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sucrase-isomaltase, intestinal between cysteines 93 and 106 (60 and 73 respectively in this structure).

Details

Redox score ?
68
PDB code
3lpp
Structure name
crystal complex of n-terminal sucrase-isomaltase with kotalanol
Structure deposition date
2010-02-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14410
Residue number A
93
Residue number B
106
Peptide name
Sucrase-isomaltase, intestinal

Ligandability

Cysteine 93 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 106 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sucrase-isomaltase, intestinal between cysteines 77 and 88 (44 and 55 respectively in this structure).

Details

Redox score ?
65
PDB code
3lpp
Structure name
crystal complex of n-terminal sucrase-isomaltase with kotalanol
Structure deposition date
2010-02-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14410
Residue number A
77
Residue number B
88
Peptide name
Sucrase-isomaltase, intestinal

Ligandability

Cysteine 77 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 88 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sucrase-isomaltase, intestinal between cysteines 63 and 88 (30 and 55 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
60
PDB code
3lpp
Structure name
crystal complex of n-terminal sucrase-isomaltase with kotalanol
Structure deposition date
2010-02-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14410
Residue number A
63
Residue number B
88
Peptide name
Sucrase-isomaltase, intestinal

Ligandability

Cysteine 63 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 88 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sucrase-isomaltase, intestinal between cysteines 88 and 94 (55 and 61 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
3lpp
Structure name
crystal complex of n-terminal sucrase-isomaltase with kotalanol
Structure deposition date
2010-02-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14410
Residue number A
88
Residue number B
94
Peptide name
Sucrase-isomaltase, intestinal

Ligandability

Cysteine 88 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 94 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sucrase-isomaltase, intestinal between cysteines 63 and 106 (30 and 73 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
3lpp
Structure name
crystal complex of n-terminal sucrase-isomaltase with kotalanol
Structure deposition date
2010-02-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14410
Residue number A
63
Residue number B
106
Peptide name
Sucrase-isomaltase, intestinal

Ligandability

Cysteine 63 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 106 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sucrase-isomaltase, intestinal between cysteines 94 and 106 (61 and 73 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
3lpp
Structure name
crystal complex of n-terminal sucrase-isomaltase with kotalanol
Structure deposition date
2010-02-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14410
Residue number A
94
Residue number B
106
Peptide name
Sucrase-isomaltase, intestinal

Ligandability

Cysteine 94 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 106 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sucrase-isomaltase, intestinal between cysteines 63 and 93 (30 and 60 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
3lpp
Structure name
crystal complex of n-terminal sucrase-isomaltase with kotalanol
Structure deposition date
2010-02-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14410
Residue number A
63
Residue number B
93
Peptide name
Sucrase-isomaltase, intestinal

Ligandability

Cysteine 63 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 93 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sucrase-isomaltase, intestinal between cysteines 93 and 94 (60 and 61 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
3lpp
Structure name
crystal complex of n-terminal sucrase-isomaltase with kotalanol
Structure deposition date
2010-02-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14410
Residue number A
93
Residue number B
94
Peptide name
Sucrase-isomaltase, intestinal

Ligandability

Cysteine 93 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 94 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sucrase-isomaltase, intestinal between cysteines 77 and 94 (44 and 61 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
3lpo
Structure name
crystal structure of the n-terminal domain of sucrase-isomaltase
Structure deposition date
2010-02-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14410
Residue number A
77
Residue number B
94
Peptide name
Sucrase-isomaltase, intestinal

Ligandability

Cysteine 77 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 94 of Sucrase-isomaltase, intestinal

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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