Semaphorin-6A
Intramolecular
Cysteine 521 and cysteine 568
Cysteine 107 and cysteine 117
Cysteine 515 and cysteine 533
Cysteine 525 and cysteine 542
Cysteine 283 and cysteine 328
Cysteine 477 and cysteine 506
Cysteine 258 and cysteine 369
Cysteine 135 and cysteine 144
Cysteine 515 and cysteine 542
Cysteine 533 and cysteine 542
More...Cysteine 525 and cysteine 533
Cysteine 515 and cysteine 525
Cysteine 368 and cysteine 369
Cysteine 135 and cysteine 165
Cysteine 144 and cysteine 165
Cysteine 258 and cysteine 368
Cysteine 521 and cysteine 542
Cysteine 525 and cysteine 568
Cysteine 521 and cysteine 525
3okw B 521 B 568
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 521 and 568.
Details
Redox score ?
94
PDB code
3okw
Structure name
mouse semaphorin 6a, extracellular domains 1-2
Structure deposition date
2010-08-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35464
Residue number A
521
Residue number B
568
Peptide name
Semaphorin-6A
Ligandability
Cysteine 521 of Semaphorin-6A
Cysteine 568 of Semaphorin-6A
6wts B 107 B 117
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 107 and 117.
Details
Redox score ?
85
PDB code
6wts
Structure name
cryoem structure of the c
Structure deposition date
2020-05-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H2E6
Residue number A
107
Residue number B
117
Peptide name
Semaphorin-6A
Ligandability
Cysteine 107 of Semaphorin-6A
Cysteine 117 of Semaphorin-6A
3afc A 515 A 533
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 515 and 533.
Details
Redox score ?
85
PDB code
3afc
Structure name
mouse semaphorin 6a extracellular domain
Structure deposition date
2010-02-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35464
Residue number A
515
Residue number B
533
Peptide name
Semaphorin-6A
Ligandability
Cysteine 515 of Semaphorin-6A
Cysteine 533 of Semaphorin-6A
6wts A 525 A 542
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 525 and 542.
Details
Redox score ?
84
PDB code
6wts
Structure name
cryoem structure of the c
Structure deposition date
2020-05-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H2E6
Residue number A
525
Residue number B
542
Peptide name
Semaphorin-6A
Ligandability
Cysteine 525 of Semaphorin-6A
Cysteine 542 of Semaphorin-6A
6wts A 283 A 328
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 283 and 328.
Details
Redox score ?
82
PDB code
6wts
Structure name
cryoem structure of the c
Structure deposition date
2020-05-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H2E6
Residue number A
283
Residue number B
328
Peptide name
Semaphorin-6A
Ligandability
Cysteine 283 of Semaphorin-6A
Cysteine 328 of Semaphorin-6A
6wts A 477 A 506
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 477 and 506.
Details
Redox score ?
82
PDB code
6wts
Structure name
cryoem structure of the c
Structure deposition date
2020-05-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H2E6
Residue number A
477
Residue number B
506
Peptide name
Semaphorin-6A
Ligandability
Cysteine 477 of Semaphorin-6A
Cysteine 506 of Semaphorin-6A
6wts B 258 B 369
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 258 and 369.
Details
Redox score ?
81
PDB code
6wts
Structure name
cryoem structure of the c
Structure deposition date
2020-05-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H2E6
Residue number A
258
Residue number B
369
Peptide name
Semaphorin-6A
Ligandability
Cysteine 258 of Semaphorin-6A
Cysteine 369 of Semaphorin-6A
6wts B 135 B 144
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 135 and 144.
Details
Redox score ?
79
PDB code
6wts
Structure name
cryoem structure of the c
Structure deposition date
2020-05-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H2E6
Residue number A
135
Residue number B
144
Peptide name
Semaphorin-6A
Ligandability
Cysteine 135 of Semaphorin-6A
Cysteine 144 of Semaphorin-6A
6wts A 515 A 542
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 515 and 542.
Details
Redox score ?
67
PDB code
6wts
Structure name
cryoem structure of the c
Structure deposition date
2020-05-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H2E6
Residue number A
515
Residue number B
542
Peptide name
Semaphorin-6A
Ligandability
Cysteine 515 of Semaphorin-6A
Cysteine 542 of Semaphorin-6A
6wts A 533 A 542
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 533 and 542.
Details
Redox score ?
66
PDB code
6wts
Structure name
cryoem structure of the c
Structure deposition date
2020-05-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H2E6
Residue number A
533
Residue number B
542
Peptide name
Semaphorin-6A
Ligandability
Cysteine 533 of Semaphorin-6A
Cysteine 542 of Semaphorin-6A
6wts A 525 A 533
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 525 and 533. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
6wts
Structure name
cryoem structure of the c
Structure deposition date
2020-05-03
Thiol separation (Å)
6
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H2E6
Residue number A
525
Residue number B
533
Peptide name
Semaphorin-6A
Ligandability
Cysteine 525 of Semaphorin-6A
Cysteine 533 of Semaphorin-6A
6wts A 515 A 525
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 515 and 525. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
6wts
Structure name
cryoem structure of the c
Structure deposition date
2020-05-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H2E6
Residue number A
515
Residue number B
525
Peptide name
Semaphorin-6A
Ligandability
Cysteine 515 of Semaphorin-6A
Cysteine 525 of Semaphorin-6A
3afc B 368 B 369
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 368 and 369. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
3afc
Structure name
mouse semaphorin 6a extracellular domain
Structure deposition date
2010-02-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
nan
Peptide accession
O35464
Residue number A
368
Residue number B
369
Peptide name
Semaphorin-6A
Ligandability
Cysteine 368 of Semaphorin-6A
Cysteine 369 of Semaphorin-6A
6wts B 135 B 165
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 135 and 165. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
6wts
Structure name
cryoem structure of the c
Structure deposition date
2020-05-03
Thiol separation (Å)
6
Half-sphere exposure sum ?
90
Minimum pKa ?
12
% buried
nan
Peptide accession
Q9H2E6
Residue number A
135
Residue number B
165
Peptide name
Semaphorin-6A
Ligandability
Cysteine 135 of Semaphorin-6A
Cysteine 165 of Semaphorin-6A
6wts B 144 B 165
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 144 and 165. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
6wts
Structure name
cryoem structure of the c
Structure deposition date
2020-05-03
Thiol separation (Å)
6
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
nan
Peptide accession
Q9H2E6
Residue number A
144
Residue number B
165
Peptide name
Semaphorin-6A
Ligandability
Cysteine 144 of Semaphorin-6A
Cysteine 165 of Semaphorin-6A
3okw B 258 B 368
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 258 and 368. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
3okw
Structure name
mouse semaphorin 6a, extracellular domains 1-2
Structure deposition date
2010-08-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
nan
Peptide accession
O35464
Residue number A
258
Residue number B
368
Peptide name
Semaphorin-6A
Ligandability
Cysteine 258 of Semaphorin-6A
Cysteine 368 of Semaphorin-6A
3afc A 521 A 542
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 521 and 542. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
3afc
Structure name
mouse semaphorin 6a extracellular domain
Structure deposition date
2010-02-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35464
Residue number A
521
Residue number B
542
Peptide name
Semaphorin-6A
Ligandability
Cysteine 521 of Semaphorin-6A
Cysteine 542 of Semaphorin-6A
3afc A 525 A 568
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 525 and 568. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
3afc
Structure name
mouse semaphorin 6a extracellular domain
Structure deposition date
2010-02-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35464
Residue number A
525
Residue number B
568
Peptide name
Semaphorin-6A
Ligandability
Cysteine 525 of Semaphorin-6A
Cysteine 568 of Semaphorin-6A
3okw A 521 A 525
A redox-regulated disulphide may form within Semaphorin-6A between cysteines 521 and 525. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
3okw
Structure name
mouse semaphorin 6a, extracellular domains 1-2
Structure deposition date
2010-08-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
O35464
Residue number A
521
Residue number B
525
Peptide name
Semaphorin-6A
Ligandability
Cysteine 521 of Semaphorin-6A
Cysteine 525 of Semaphorin-6A
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