Testin
Intramolecular
Cysteine 301 and cysteine 304
Cysteine 412 and cysteine 416
Cysteine 328 and cysteine 331
Cysteine 391 and cysteine 416
Cysteine 331 and cysteine 349
Cysteine 331 and cysteine 352
Cysteine 328 and cysteine 352
Cysteine 394 and cysteine 416
Cysteine 391 and cysteine 394
Cysteine 328 and cysteine 349
More...Cysteine 393 and cysteine 416
Cysteine 349 and cysteine 352
Cysteine 391 and cysteine 412
Cysteine 394 and cysteine 412
Cysteine 361 and cysteine 364
Cysteine 364 and cysteine 388
Cysteine 391 and cysteine 393
Cysteine 393 and cysteine 394
Cysteine 393 and cysteine 412
Cysteine 361 and cysteine 388
Cysteine 327 and cysteine 331
Cysteine 327 and cysteine 328
Cysteine 388 and cysteine 397
2xqn T 301 T 304
A redox-regulated disulphide may form within Testin between cysteines 301 and 304.
Details
Redox score ?
89
PDB code
2xqn
Structure name
complex of the 2nd and 3rd lim domains of tes with the evh1 domain of mena and the n-terminal domain of actin-like protein arp7a
Structure deposition date
2010-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
5
% buried
8
Peptide accession
Q9UGI8
Residue number A
301
Residue number B
304
Peptide name
Testin
Ligandability
Cysteine 301 of Testin
Cysteine 304 of Testin
2xqn T 412 T 416
A redox-regulated disulphide may form within Testin between cysteines 412 and 416.
Details
Redox score ?
88
PDB code
2xqn
Structure name
complex of the 2nd and 3rd lim domains of tes with the evh1 domain of mena and the n-terminal domain of actin-like protein arp7a
Structure deposition date
2010-09-03
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
5
% buried
7
Peptide accession
Q9UGI8
Residue number A
412
Residue number B
416
Peptide name
Testin
Ligandability
Cysteine 412 of Testin
Cysteine 416 of Testin
2xqn T 328 T 331
A redox-regulated disulphide may form within Testin between cysteines 328 and 331.
Details
Redox score ?
86
PDB code
2xqn
Structure name
complex of the 2nd and 3rd lim domains of tes with the evh1 domain of mena and the n-terminal domain of actin-like protein arp7a
Structure deposition date
2010-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
7
Peptide accession
Q9UGI8
Residue number A
328
Residue number B
331
Peptide name
Testin
Ligandability
Cysteine 328 of Testin
Cysteine 331 of Testin
2xqn T 391 T 416
A redox-regulated disulphide may form within Testin between cysteines 391 and 416.
Details
Redox score ?
85
PDB code
2xqn
Structure name
complex of the 2nd and 3rd lim domains of tes with the evh1 domain of mena and the n-terminal domain of actin-like protein arp7a
Structure deposition date
2010-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
5
% buried
22
Peptide accession
Q9UGI8
Residue number A
391
Residue number B
416
Peptide name
Testin
Ligandability
Cysteine 391 of Testin
Cysteine 416 of Testin
2xqn T 331 T 349
A redox-regulated disulphide may form within Testin between cysteines 331 and 349.
Details
Redox score ?
85
PDB code
2xqn
Structure name
complex of the 2nd and 3rd lim domains of tes with the evh1 domain of mena and the n-terminal domain of actin-like protein arp7a
Structure deposition date
2010-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
6
% buried
6
Peptide accession
Q9UGI8
Residue number A
331
Residue number B
349
Peptide name
Testin
Ligandability
Cysteine 331 of Testin
Cysteine 349 of Testin
2xqn T 331 T 352
A redox-regulated disulphide may form within Testin between cysteines 331 and 352.
Details
Redox score ?
85
PDB code
2xqn
Structure name
complex of the 2nd and 3rd lim domains of tes with the evh1 domain of mena and the n-terminal domain of actin-like protein arp7a
Structure deposition date
2010-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
6
% buried
0
Peptide accession
Q9UGI8
Residue number A
331
Residue number B
352
Peptide name
Testin
Ligandability
Cysteine 331 of Testin
Cysteine 352 of Testin
2xqn T 328 T 352
A redox-regulated disulphide may form within Testin between cysteines 328 and 352.
Details
Redox score ?
84
PDB code
2xqn
Structure name
complex of the 2nd and 3rd lim domains of tes with the evh1 domain of mena and the n-terminal domain of actin-like protein arp7a
Structure deposition date
2010-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
7
% buried
7
Peptide accession
Q9UGI8
Residue number A
328
Residue number B
352
Peptide name
Testin
Ligandability
Cysteine 328 of Testin
Cysteine 352 of Testin
2xqn T 394 T 416
A redox-regulated disulphide may form within Testin between cysteines 394 and 416.
Details
Redox score ?
82
PDB code
2xqn
Structure name
complex of the 2nd and 3rd lim domains of tes with the evh1 domain of mena and the n-terminal domain of actin-like protein arp7a
Structure deposition date
2010-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
5
% buried
9
Peptide accession
Q9UGI8
Residue number A
394
Residue number B
416
Peptide name
Testin
Ligandability
Cysteine 394 of Testin
Cysteine 416 of Testin
2iyb H 391 H 394
A redox-regulated disulphide may form within Testin between cysteines 391 and 394.
Details
Redox score ?
80
PDB code
2iyb
Structure name
structure of complex between the 3rd lim domain of tes and the evh1 domain of mena
Structure deposition date
2006-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
6
% buried
30
Peptide accession
Q9UGI8
Residue number A
391
Residue number B
394
Peptide name
Testin
Ligandability
Cysteine 391 of Testin
Cysteine 394 of Testin
2xqn T 328 T 349
A redox-regulated disulphide may form within Testin between cysteines 328 and 349.
Details
Redox score ?
80
PDB code
2xqn
Structure name
complex of the 2nd and 3rd lim domains of tes with the evh1 domain of mena and the n-terminal domain of actin-like protein arp7a
Structure deposition date
2010-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
7
% buried
13
Peptide accession
Q9UGI8
Residue number A
328
Residue number B
349
Peptide name
Testin
Ligandability
Cysteine 328 of Testin
Cysteine 349 of Testin
2iyb E 393 E 416
A redox-regulated disulphide may form within Testin between cysteines 393 and 416.
Details
Redox score ?
77
PDB code
2iyb
Structure name
structure of complex between the 3rd lim domain of tes and the evh1 domain of mena
Structure deposition date
2006-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
8
% buried
22
Peptide accession
Q9UGI8
Residue number A
393
Residue number B
416
Peptide name
Testin
Ligandability
Cysteine 393 of Testin
Cysteine 416 of Testin
2xqn T 349 T 352
A redox-regulated disulphide may form within Testin between cysteines 349 and 352.
Details
Redox score ?
76
PDB code
2xqn
Structure name
complex of the 2nd and 3rd lim domains of tes with the evh1 domain of mena and the n-terminal domain of actin-like protein arp7a
Structure deposition date
2010-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
6
Peptide accession
Q9UGI8
Residue number A
349
Residue number B
352
Peptide name
Testin
Ligandability
Cysteine 349 of Testin
Cysteine 352 of Testin
2xqn T 391 T 412
A redox-regulated disulphide may form within Testin between cysteines 391 and 412.
Details
Redox score ?
75
PDB code
2xqn
Structure name
complex of the 2nd and 3rd lim domains of tes with the evh1 domain of mena and the n-terminal domain of actin-like protein arp7a
Structure deposition date
2010-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
26
Peptide accession
Q9UGI8
Residue number A
391
Residue number B
412
Peptide name
Testin
Ligandability
Cysteine 391 of Testin
Cysteine 412 of Testin
2xqn T 394 T 412
A redox-regulated disulphide may form within Testin between cysteines 394 and 412.
Details
Redox score ?
74
PDB code
2xqn
Structure name
complex of the 2nd and 3rd lim domains of tes with the evh1 domain of mena and the n-terminal domain of actin-like protein arp7a
Structure deposition date
2010-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
12
Peptide accession
Q9UGI8
Residue number A
394
Residue number B
412
Peptide name
Testin
Ligandability
Cysteine 394 of Testin
Cysteine 412 of Testin
2iyb E 361 E 364
A redox-regulated disulphide may form within Testin between cysteines 361 and 364.
Details
Redox score ?
71
PDB code
2iyb
Structure name
structure of complex between the 3rd lim domain of tes and the evh1 domain of mena
Structure deposition date
2006-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9UGI8
Residue number A
361
Residue number B
364
Peptide name
Testin
Ligandability
Cysteine 361 of Testin
Cysteine 364 of Testin
2iyb G 364 G 388
A redox-regulated disulphide may form within Testin between cysteines 364 and 388.
Details
Redox score ?
69
PDB code
2iyb
Structure name
structure of complex between the 3rd lim domain of tes and the evh1 domain of mena
Structure deposition date
2006-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
9
% buried
58
Peptide accession
Q9UGI8
Residue number A
364
Residue number B
388
Peptide name
Testin
Ligandability
Cysteine 364 of Testin
Cysteine 388 of Testin
2xqn T 391 T 393
A redox-regulated disulphide may form within Testin between cysteines 391 and 393.
Details
Redox score ?
67
PDB code
2xqn
Structure name
complex of the 2nd and 3rd lim domains of tes with the evh1 domain of mena and the n-terminal domain of actin-like protein arp7a
Structure deposition date
2010-09-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
26
Peptide accession
Q9UGI8
Residue number A
391
Residue number B
393
Peptide name
Testin
Ligandability
Cysteine 391 of Testin
Cysteine 393 of Testin
2iyb E 393 E 394
A redox-regulated disulphide may form within Testin between cysteines 393 and 394. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
2iyb
Structure name
structure of complex between the 3rd lim domain of tes and the evh1 domain of mena
Structure deposition date
2006-07-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
24
Peptide accession
Q9UGI8
Residue number A
393
Residue number B
394
Peptide name
Testin
Ligandability
Cysteine 393 of Testin
Cysteine 394 of Testin
2xqn T 393 T 412
A redox-regulated disulphide may form within Testin between cysteines 393 and 412. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
2xqn
Structure name
complex of the 2nd and 3rd lim domains of tes with the evh1 domain of mena and the n-terminal domain of actin-like protein arp7a
Structure deposition date
2010-09-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
10
Peptide accession
Q9UGI8
Residue number A
393
Residue number B
412
Peptide name
Testin
Ligandability
Cysteine 393 of Testin
Cysteine 412 of Testin
2xqn T 361 T 388
A redox-regulated disulphide may form within Testin between cysteines 361 and 388. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
2xqn
Structure name
complex of the 2nd and 3rd lim domains of tes with the evh1 domain of mena and the n-terminal domain of actin-like protein arp7a
Structure deposition date
2010-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
18
% buried
nan
Peptide accession
Q9UGI8
Residue number A
361
Residue number B
388
Peptide name
Testin
Ligandability
Cysteine 361 of Testin
Cysteine 388 of Testin
2xqn T 327 T 331
A redox-regulated disulphide may form within Testin between cysteines 327 and 331. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
2xqn
Structure name
complex of the 2nd and 3rd lim domains of tes with the evh1 domain of mena and the n-terminal domain of actin-like protein arp7a
Structure deposition date
2010-09-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
6
% buried
10
Peptide accession
Q9UGI8
Residue number A
327
Residue number B
331
Peptide name
Testin
Ligandability
Cysteine 327 of Testin
Cysteine 331 of Testin
2xqn T 327 T 328
A redox-regulated disulphide may form within Testin between cysteines 327 and 328. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
2xqn
Structure name
complex of the 2nd and 3rd lim domains of tes with the evh1 domain of mena and the n-terminal domain of actin-like protein arp7a
Structure deposition date
2010-09-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
7
% buried
16
Peptide accession
Q9UGI8
Residue number A
327
Residue number B
328
Peptide name
Testin
Ligandability
Cysteine 327 of Testin
Cysteine 328 of Testin
2iyb E 388 E 397
A redox-regulated disulphide may form within Testin between cysteines 388 and 397. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
2iyb
Structure name
structure of complex between the 3rd lim domain of tes and the evh1 domain of mena
Structure deposition date
2006-07-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
26
Peptide accession
Q9UGI8
Residue number A
388
Residue number B
397
Peptide name
Testin
Ligandability
Cysteine 388 of Testin
Cysteine 397 of Testin
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