ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Semaphorin-3A

Intramolecular
Cysteine 524 and cysteine 567
Cysteine 527 and cysteine 542
Cysteine 103 and cysteine 114
Cysteine 517 and cysteine 535
Cysteine 293 and cysteine 341
Cysteine 269 and cysteine 381
Cysteine 132 and cysteine 141
Cysteine 517 and cysteine 542
Cysteine 535 and cysteine 542
Cysteine 528 and cysteine 567
More...
Cysteine 527 and cysteine 535
Cysteine 517 and cysteine 527
Cysteine 524 and cysteine 528
Cysteine 524 and cysteine 527
Cysteine 527 and cysteine 567
Cysteine 524 and cysteine 542
Cysteine 542 and cysteine 567
Cysteine 527 and cysteine 528
Cysteine 528 and cysteine 542
A redox-regulated disulphide may form within Semaphorin-3A between cysteines 524 and 567.

Details

Redox score ?
88
PDB code
4gz8
Structure name
mouse semaphorin 3a, domains sema-psi-ig
Structure deposition date
2012-09-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08665
Residue number A
524
Residue number B
567
Peptide name
Semaphorin-3A

Ligandability

Cysteine 524 of Semaphorin-3A

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 567 of Semaphorin-3A

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 Semaphorin-3A between cysteines 527 and 542.

Details

Redox score ?
85
PDB code
4gz8
Structure name
mouse semaphorin 3a, domains sema-psi-ig
Structure deposition date
2012-09-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08665
Residue number A
527
Residue number B
542
Peptide name
Semaphorin-3A

Ligandability

Cysteine 527 of Semaphorin-3A

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 542 of Semaphorin-3A

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 Semaphorin-3A between cysteines 103 and 114.

Details

Redox score ?
84
PDB code
1q47
Structure name
structure of the semaphorin 3a receptor-binding module
Structure deposition date
2003-08-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08665
Residue number A
103
Residue number B
114
Peptide name
Semaphorin-3A

Ligandability

Cysteine 103 of Semaphorin-3A

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 114 of Semaphorin-3A

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 Semaphorin-3A between cysteines 517 and 535.

Details

Redox score ?
84
PDB code
4gz8
Structure name
mouse semaphorin 3a, domains sema-psi-ig
Structure deposition date
2012-09-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08665
Residue number A
517
Residue number B
535
Peptide name
Semaphorin-3A

Ligandability

Cysteine 517 of Semaphorin-3A

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 535 of Semaphorin-3A

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 Semaphorin-3A between cysteines 293 and 341.

Details

Redox score ?
82
PDB code
1q47
Structure name
structure of the semaphorin 3a receptor-binding module
Structure deposition date
2003-08-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08665
Residue number A
293
Residue number B
341
Peptide name
Semaphorin-3A

Ligandability

Cysteine 293 of Semaphorin-3A

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 341 of Semaphorin-3A

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 Semaphorin-3A between cysteines 269 and 381.

Details

Redox score ?
80
PDB code
1q47
Structure name
structure of the semaphorin 3a receptor-binding module
Structure deposition date
2003-08-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08665
Residue number A
269
Residue number B
381
Peptide name
Semaphorin-3A

Ligandability

Cysteine 269 of Semaphorin-3A

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 381 of Semaphorin-3A

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 Semaphorin-3A between cysteines 132 and 141.

Details

Redox score ?
74
PDB code
1q47
Structure name
structure of the semaphorin 3a receptor-binding module
Structure deposition date
2003-08-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
86
Minimum pKa ?
7
% buried
98
Peptide accession
O08665
Residue number A
132
Residue number B
141
Peptide name
Semaphorin-3A

Ligandability

Cysteine 132 of Semaphorin-3A

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 141 of Semaphorin-3A

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 Semaphorin-3A between cysteines 517 and 542.

Details

Redox score ?
70
PDB code
4gz8
Structure name
mouse semaphorin 3a, domains sema-psi-ig
Structure deposition date
2012-09-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08665
Residue number A
517
Residue number B
542
Peptide name
Semaphorin-3A

Ligandability

Cysteine 517 of Semaphorin-3A

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 542 of Semaphorin-3A

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 Semaphorin-3A between cysteines 535 and 542.

Details

Redox score ?
69
PDB code
4gz8
Structure name
mouse semaphorin 3a, domains sema-psi-ig
Structure deposition date
2012-09-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08665
Residue number A
535
Residue number B
542
Peptide name
Semaphorin-3A

Ligandability

Cysteine 535 of Semaphorin-3A

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 542 of Semaphorin-3A

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 Semaphorin-3A between cysteines 528 and 567.

Details

Redox score ?
67
PDB code
4gz8
Structure name
mouse semaphorin 3a, domains sema-psi-ig
Structure deposition date
2012-09-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
nan
Peptide accession
O08665
Residue number A
528
Residue number B
567
Peptide name
Semaphorin-3A

Ligandability

Cysteine 528 of Semaphorin-3A

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 567 of Semaphorin-3A

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 Semaphorin-3A between cysteines 527 and 535.

Details

Redox score ?
60
PDB code
4gz8
Structure name
mouse semaphorin 3a, domains sema-psi-ig
Structure deposition date
2012-09-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08665
Residue number A
527
Residue number B
535
Peptide name
Semaphorin-3A

Ligandability

Cysteine 527 of Semaphorin-3A

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 535 of Semaphorin-3A

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 Semaphorin-3A between cysteines 517 and 527. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
4gz8
Structure name
mouse semaphorin 3a, domains sema-psi-ig
Structure deposition date
2012-09-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08665
Residue number A
517
Residue number B
527
Peptide name
Semaphorin-3A

Ligandability

Cysteine 517 of Semaphorin-3A

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 527 of Semaphorin-3A

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 Semaphorin-3A between cysteines 524 and 528. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
4gz8
Structure name
mouse semaphorin 3a, domains sema-psi-ig
Structure deposition date
2012-09-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
nan
Peptide accession
O08665
Residue number A
524
Residue number B
528
Peptide name
Semaphorin-3A

Ligandability

Cysteine 524 of Semaphorin-3A

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 528 of Semaphorin-3A

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 Semaphorin-3A between cysteines 524 and 527. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
4gz8
Structure name
mouse semaphorin 3a, domains sema-psi-ig
Structure deposition date
2012-09-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08665
Residue number A
524
Residue number B
527
Peptide name
Semaphorin-3A

Ligandability

Cysteine 524 of Semaphorin-3A

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 527 of Semaphorin-3A

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 Semaphorin-3A between cysteines 527 and 567. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
4gz8
Structure name
mouse semaphorin 3a, domains sema-psi-ig
Structure deposition date
2012-09-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08665
Residue number A
527
Residue number B
567
Peptide name
Semaphorin-3A

Ligandability

Cysteine 527 of Semaphorin-3A

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 567 of Semaphorin-3A

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 Semaphorin-3A between cysteines 524 and 542. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
4gz8
Structure name
mouse semaphorin 3a, domains sema-psi-ig
Structure deposition date
2012-09-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08665
Residue number A
524
Residue number B
542
Peptide name
Semaphorin-3A

Ligandability

Cysteine 524 of Semaphorin-3A

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 542 of Semaphorin-3A

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 Semaphorin-3A between cysteines 542 and 567. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
4gz8
Structure name
mouse semaphorin 3a, domains sema-psi-ig
Structure deposition date
2012-09-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08665
Residue number A
542
Residue number B
567
Peptide name
Semaphorin-3A

Ligandability

Cysteine 542 of Semaphorin-3A

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 567 of Semaphorin-3A

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 Semaphorin-3A between cysteines 527 and 528. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4gz8
Structure name
mouse semaphorin 3a, domains sema-psi-ig
Structure deposition date
2012-09-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
nan
Peptide accession
O08665
Residue number A
527
Residue number B
528
Peptide name
Semaphorin-3A

Ligandability

Cysteine 527 of Semaphorin-3A

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 528 of Semaphorin-3A

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 Semaphorin-3A between cysteines 528 and 542. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
4gz8
Structure name
mouse semaphorin 3a, domains sema-psi-ig
Structure deposition date
2012-09-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
nan
Peptide accession
O08665
Residue number A
528
Residue number B
542
Peptide name
Semaphorin-3A

Ligandability

Cysteine 528 of Semaphorin-3A

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 542 of Semaphorin-3A

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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