Fibronectin
Intramolecular
Cysteine 518 and cysteine 545
Cysteine 543 and cysteine 555
Cysteine 333 and cysteine 342
Cysteine 434 and cysteine 461
Cysteine 561 and cysteine 589
Cysteine 308 and cysteine 335
Cysteine 374 and cysteine 401
Cysteine 470 and cysteine 498
Cysteine 587 and cysteine 599
Cysteine 496 and cysteine 508
More...Cysteine 360 and cysteine 386
Cysteine 420 and cysteine 446
Cysteine 420 and cysteine 461
Cysteine 360 and cysteine 401
Cysteine 420 and cysteine 434
Cysteine 386 and cysteine 401
Cysteine 446 and cysteine 461
Cysteine 360 and cysteine 374
Cysteine 434 and cysteine 446
Cysteine 374 and cysteine 386
Cysteine 543 and cysteine 545
Cysteine 518 and cysteine 543
Cysteine 308 and cysteine 342
Cysteine 561 and cysteine 599
Cysteine 561 and cysteine 587
Cysteine 470 and cysteine 496
Cysteine 470 and cysteine 508
Cysteine 308 and cysteine 333
3m7p A 518 A 545
A redox-regulated disulphide may form within Fibronectin between cysteines 518 and 545.
Details
Redox score ?
88
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
0
Peptide accession
B7ZLE5
Residue number A
518
Residue number B
545
Peptide name
Fibronectin
Ligandability
Cysteine 518 of Fibronectin
Cysteine 545 of Fibronectin
3m7p A 543 A 555
A redox-regulated disulphide may form within Fibronectin between cysteines 543 and 555.
Details
Redox score ?
88
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
41
Minimum pKa ?
9
% buried
0
Peptide accession
B7ZLE5
Residue number A
543
Residue number B
555
Peptide name
Fibronectin
Ligandability
Cysteine 543 of Fibronectin
Cysteine 555 of Fibronectin
3m7p A 333 A 342
A redox-regulated disulphide may form within Fibronectin between cysteines 333 and 342.
Details
Redox score ?
87
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
19
Peptide accession
B7ZLE5
Residue number A
333
Residue number B
342
Peptide name
Fibronectin
Ligandability
Cysteine 333 of Fibronectin
Cysteine 342 of Fibronectin
3m7p A 434 A 461
A redox-regulated disulphide may form within Fibronectin between cysteines 434 and 461.
Details
Redox score ?
84
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
434
Residue number B
461
Peptide name
Fibronectin
Ligandability
Cysteine 434 of Fibronectin
Cysteine 461 of Fibronectin
3m7p A 561 A 589
A redox-regulated disulphide may form within Fibronectin between cysteines 561 and 589.
Details
Redox score ?
84
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
561
Residue number B
589
Peptide name
Fibronectin
Ligandability
Cysteine 561 of Fibronectin
Cysteine 589 of Fibronectin
3m7p A 308 A 335
A redox-regulated disulphide may form within Fibronectin between cysteines 308 and 335.
Details
Redox score ?
83
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
308
Residue number B
335
Peptide name
Fibronectin
Ligandability
Cysteine 308 of Fibronectin
Cysteine 335 of Fibronectin
3m7p A 374 A 401
A redox-regulated disulphide may form within Fibronectin between cysteines 374 and 401.
Details
Redox score ?
83
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
374
Residue number B
401
Peptide name
Fibronectin
Ligandability
Cysteine 374 of Fibronectin
Cysteine 401 of Fibronectin
3m7p A 470 A 498
A redox-regulated disulphide may form within Fibronectin between cysteines 470 and 498.
Details
Redox score ?
82
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
470
Residue number B
498
Peptide name
Fibronectin
Ligandability
Cysteine 470 of Fibronectin
Cysteine 498 of Fibronectin
3m7p A 587 A 599
A redox-regulated disulphide may form within Fibronectin between cysteines 587 and 599.
Details
Redox score ?
82
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
587
Residue number B
599
Peptide name
Fibronectin
Ligandability
Cysteine 587 of Fibronectin
Cysteine 599 of Fibronectin
3m7p A 496 A 508
A redox-regulated disulphide may form within Fibronectin between cysteines 496 and 508.
Details
Redox score ?
81
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
496
Residue number B
508
Peptide name
Fibronectin
Ligandability
Cysteine 496 of Fibronectin
Cysteine 508 of Fibronectin
3m7p A 360 A 386
A redox-regulated disulphide may form within Fibronectin between cysteines 360 and 386.
Details
Redox score ?
80
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
91
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
360
Residue number B
386
Peptide name
Fibronectin
Ligandability
Cysteine 360 of Fibronectin
Cysteine 386 of Fibronectin
3m7p A 420 A 446
A redox-regulated disulphide may form within Fibronectin between cysteines 420 and 446.
Details
Redox score ?
77
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
420
Residue number B
446
Peptide name
Fibronectin
Ligandability
Cysteine 420 of Fibronectin
Cysteine 446 of Fibronectin
3m7p A 420 A 461
A redox-regulated disulphide may form within Fibronectin between cysteines 420 and 461.
Details
Redox score ?
73
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
420
Residue number B
461
Peptide name
Fibronectin
Ligandability
Cysteine 420 of Fibronectin
Cysteine 461 of Fibronectin
3m7p A 360 A 401
A redox-regulated disulphide may form within Fibronectin between cysteines 360 and 401.
Details
Redox score ?
72
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
360
Residue number B
401
Peptide name
Fibronectin
Ligandability
Cysteine 360 of Fibronectin
Cysteine 401 of Fibronectin
3m7p A 420 A 434
A redox-regulated disulphide may form within Fibronectin between cysteines 420 and 434.
Details
Redox score ?
72
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
420
Residue number B
434
Peptide name
Fibronectin
Ligandability
Cysteine 420 of Fibronectin
Cysteine 434 of Fibronectin
3m7p A 386 A 401
A redox-regulated disulphide may form within Fibronectin between cysteines 386 and 401.
Details
Redox score ?
71
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
386
Residue number B
401
Peptide name
Fibronectin
Ligandability
Cysteine 386 of Fibronectin
Cysteine 401 of Fibronectin
3m7p A 446 A 461
A redox-regulated disulphide may form within Fibronectin between cysteines 446 and 461.
Details
Redox score ?
70
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
446
Residue number B
461
Peptide name
Fibronectin
Ligandability
Cysteine 446 of Fibronectin
Cysteine 461 of Fibronectin
3m7p A 360 A 374
A redox-regulated disulphide may form within Fibronectin between cysteines 360 and 374.
Details
Redox score ?
70
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
360
Residue number B
374
Peptide name
Fibronectin
Ligandability
Cysteine 360 of Fibronectin
Cysteine 374 of Fibronectin
3m7p A 434 A 446
A redox-regulated disulphide may form within Fibronectin between cysteines 434 and 446.
Details
Redox score ?
66
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
434
Residue number B
446
Peptide name
Fibronectin
Ligandability
Cysteine 434 of Fibronectin
Cysteine 446 of Fibronectin
3m7p A 374 A 386
A redox-regulated disulphide may form within Fibronectin between cysteines 374 and 386.
Details
Redox score ?
65
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
374
Residue number B
386
Peptide name
Fibronectin
Ligandability
Cysteine 374 of Fibronectin
Cysteine 386 of Fibronectin
3m7p A 543 A 545
A redox-regulated disulphide may form within Fibronectin between cysteines 543 and 545. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
11
% buried
0
Peptide accession
B7ZLE5
Residue number A
543
Residue number B
545
Peptide name
Fibronectin
Ligandability
Cysteine 543 of Fibronectin
Cysteine 545 of Fibronectin
3m7p A 518 A 543
A redox-regulated disulphide may form within Fibronectin between cysteines 518 and 543. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
0
Peptide accession
B7ZLE5
Residue number A
518
Residue number B
543
Peptide name
Fibronectin
Ligandability
Cysteine 518 of Fibronectin
Cysteine 543 of Fibronectin
3m7p A 308 A 342
A redox-regulated disulphide may form within Fibronectin between cysteines 308 and 342. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
nan
Peptide accession
B7ZLE5
Residue number A
308
Residue number B
342
Peptide name
Fibronectin
Ligandability
Cysteine 308 of Fibronectin
Cysteine 342 of Fibronectin
3m7p A 561 A 599
A redox-regulated disulphide may form within Fibronectin between cysteines 561 and 599. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
561
Residue number B
599
Peptide name
Fibronectin
Ligandability
Cysteine 561 of Fibronectin
Cysteine 599 of Fibronectin
3m7p A 561 A 587
A redox-regulated disulphide may form within Fibronectin between cysteines 561 and 587. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
561
Residue number B
587
Peptide name
Fibronectin
Ligandability
Cysteine 561 of Fibronectin
Cysteine 587 of Fibronectin
3m7p A 470 A 496
A redox-regulated disulphide may form within Fibronectin between cysteines 470 and 496. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
470
Residue number B
496
Peptide name
Fibronectin
Ligandability
Cysteine 470 of Fibronectin
Cysteine 496 of Fibronectin
3m7p A 470 A 508
A redox-regulated disulphide may form within Fibronectin between cysteines 470 and 508. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLE5
Residue number A
470
Residue number B
508
Peptide name
Fibronectin
Ligandability
Cysteine 470 of Fibronectin
Cysteine 508 of Fibronectin
3m7p A 308 A 333
A redox-regulated disulphide may form within Fibronectin between cysteines 308 and 333. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
3m7p
Structure name
fibronectin fragment
Structure deposition date
2010-03-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
12
% buried
nan
Peptide accession
B7ZLE5
Residue number A
308
Residue number B
333
Peptide name
Fibronectin
Ligandability
Cysteine 308 of Fibronectin
Cysteine 333 of Fibronectin
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