ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Semaphorin-7A

Intramolecular
Cysteine 120 and cysteine 126
Cysteine 500 and cysteine 541
Cysteine 587 and cysteine 596
Cysteine 503 and cysteine 518
Cysteine 266 and cysteine 366
Cysteine 493 and cysteine 511
Cysteine 566 and cysteine 613
Cysteine 291 and cysteine 335
Cysteine 143 and cysteine 152
Cysteine 493 and cysteine 518
More...
Cysteine 596 and cysteine 613
Cysteine 511 and cysteine 518
Cysteine 566 and cysteine 596
Cysteine 493 and cysteine 503
Cysteine 500 and cysteine 503
Cysteine 503 and cysteine 511
Cysteine 503 and cysteine 541
Cysteine 587 and cysteine 613
Cysteine 566 and cysteine 587
Cysteine 500 and cysteine 518
Cysteine 518 and cysteine 541
A redox-regulated disulphide may form within Semaphorin-7A between cysteines 120 and 126.

Details

Redox score ?
88
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
120
Residue number B
126
Peptide name
Semaphorin-7A

Ligandability

Cysteine 120 of Semaphorin-7A

Cysteine 126 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 500 and 541.

Details

Redox score ?
87
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
500
Residue number B
541
Peptide name
Semaphorin-7A

Ligandability

Cysteine 500 of Semaphorin-7A

Cysteine 541 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 587 and 596.

Details

Redox score ?
84
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
587
Residue number B
596
Peptide name
Semaphorin-7A

Ligandability

Cysteine 587 of Semaphorin-7A

Cysteine 596 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 503 and 518.

Details

Redox score ?
84
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
503
Residue number B
518
Peptide name
Semaphorin-7A

Ligandability

Cysteine 503 of Semaphorin-7A

Cysteine 518 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 266 and 366.

Details

Redox score ?
83
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
266
Residue number B
366
Peptide name
Semaphorin-7A

Ligandability

Cysteine 266 of Semaphorin-7A

Cysteine 366 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 493 and 511.

Details

Redox score ?
82
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
493
Residue number B
511
Peptide name
Semaphorin-7A

Ligandability

Cysteine 493 of Semaphorin-7A

Cysteine 511 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 566 and 613.

Details

Redox score ?
82
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
566
Residue number B
613
Peptide name
Semaphorin-7A

Ligandability

Cysteine 566 of Semaphorin-7A

Cysteine 613 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 291 and 335.

Details

Redox score ?
80
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
291
Residue number B
335
Peptide name
Semaphorin-7A

Ligandability

Cysteine 291 of Semaphorin-7A

Cysteine 335 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 143 and 152.

Details

Redox score ?
76
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
143
Residue number B
152
Peptide name
Semaphorin-7A

Ligandability

Cysteine 143 of Semaphorin-7A

Cysteine 152 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 493 and 518.

Details

Redox score ?
68
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
493
Residue number B
518
Peptide name
Semaphorin-7A

Ligandability

Cysteine 493 of Semaphorin-7A

Cysteine 518 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 596 and 613.

Details

Redox score ?
63
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
596
Residue number B
613
Peptide name
Semaphorin-7A

Ligandability

Cysteine 596 of Semaphorin-7A

Cysteine 613 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 511 and 518.

Details

Redox score ?
63
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
511
Residue number B
518
Peptide name
Semaphorin-7A

Ligandability

Cysteine 511 of Semaphorin-7A

Cysteine 518 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 566 and 596.

Details

Redox score ?
62
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
566
Residue number B
596
Peptide name
Semaphorin-7A

Ligandability

Cysteine 566 of Semaphorin-7A

Cysteine 596 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 493 and 503. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
493
Residue number B
503
Peptide name
Semaphorin-7A

Ligandability

Cysteine 493 of Semaphorin-7A

Cysteine 503 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 500 and 503. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
500
Residue number B
503
Peptide name
Semaphorin-7A

Ligandability

Cysteine 500 of Semaphorin-7A

Cysteine 503 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 503 and 511. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
503
Residue number B
511
Peptide name
Semaphorin-7A

Ligandability

Cysteine 503 of Semaphorin-7A

Cysteine 511 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 503 and 541. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
503
Residue number B
541
Peptide name
Semaphorin-7A

Ligandability

Cysteine 503 of Semaphorin-7A

Cysteine 541 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 587 and 613. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
587
Residue number B
613
Peptide name
Semaphorin-7A

Ligandability

Cysteine 587 of Semaphorin-7A

Cysteine 613 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 566 and 587. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
566
Residue number B
587
Peptide name
Semaphorin-7A

Ligandability

Cysteine 566 of Semaphorin-7A

Cysteine 587 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 500 and 518. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
500
Residue number B
518
Peptide name
Semaphorin-7A

Ligandability

Cysteine 500 of Semaphorin-7A

Cysteine 518 of Semaphorin-7A

A redox-regulated disulphide may form within Semaphorin-7A between cysteines 518 and 541. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3nvq
Structure name
molecular mechanism of guidance cue recognition
Structure deposition date
2010-07-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75326
Residue number A
518
Residue number B
541
Peptide name
Semaphorin-7A

Ligandability

Cysteine 518 of Semaphorin-7A

Cysteine 541 of Semaphorin-7A

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