ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Paxillin

Intramolecular
Cysteine 417 and cysteine 420
Cysteine 502 and cysteine 505
Cysteine 443 and cysteine 446
Cysteine 443 and cysteine 464
Cysteine 505 and cysteine 523
Cysteine 564 and cysteine 585
Cysteine 476 and cysteine 479
Cysteine 561 and cysteine 585
Cysteine 535 and cysteine 538
Cysteine 561 and cysteine 582
More...
Cysteine 561 and cysteine 564
Cysteine 476 and cysteine 499
Cysteine 479 and cysteine 499
Cysteine 446 and cysteine 464
Cysteine 502 and cysteine 523
Cysteine 564 and cysteine 582
Cysteine 582 and cysteine 585
A redox-regulated disulphide may form within Paxillin between cysteines 417 and 420 (4 and 7 respectively in this structure).

Details

Redox score ?
87
PDB code
7qb0
Structure name
solution structure of paxillin lim2/3
Structure deposition date
2021-11-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
6
% buried
0
Peptide accession
P49023
Residue number A
417
Residue number B
420
Peptide name
Paxillin

Ligandability

Cysteine 417 of Paxillin

Cysteine 420 of Paxillin

A redox-regulated disulphide may form within Paxillin between cysteines 502 and 505 (89 and 92 respectively in this structure).

Details

Redox score ?
86
PDB code
7qb0
Structure name
solution structure of paxillin lim2/3
Structure deposition date
2021-11-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
7
% buried
12
Peptide accession
P49023
Residue number A
502
Residue number B
505
Peptide name
Paxillin

Ligandability

Cysteine 502 of Paxillin

Cysteine 505 of Paxillin

A redox-regulated disulphide may form within Paxillin between cysteines 443 and 446 (30 and 33 respectively in this structure).

Details

Redox score ?
85
PDB code
7qb0
Structure name
solution structure of paxillin lim2/3
Structure deposition date
2021-11-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
7
% buried
12
Peptide accession
P49023
Residue number A
443
Residue number B
446
Peptide name
Paxillin

Ligandability

Cysteine 443 of Paxillin

Cysteine 446 of Paxillin

A redox-regulated disulphide may form within Paxillin between cysteines 443 and 464 (30 and 51 respectively in this structure).

Details

Redox score ?
85
PDB code
7qb0
Structure name
solution structure of paxillin lim2/3
Structure deposition date
2021-11-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
18
Peptide accession
P49023
Residue number A
443
Residue number B
464
Peptide name
Paxillin

Ligandability

Cysteine 443 of Paxillin

Cysteine 464 of Paxillin

A redox-regulated disulphide may form within Paxillin between cysteines 505 and 523 (92 and 110 respectively in this structure).

Details

Redox score ?
84
PDB code
7qb0
Structure name
solution structure of paxillin lim2/3
Structure deposition date
2021-11-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
10
Peptide accession
P49023
Residue number A
505
Residue number B
523
Peptide name
Paxillin

Ligandability

Cysteine 505 of Paxillin

Cysteine 523 of Paxillin

A redox-regulated disulphide may form within Paxillin between cysteines 564 and 585 (578 and 599 respectively in this structure).

Details

Redox score ?
84
PDB code
6u4m
Structure name
solution structure of paxillin lim4
Structure deposition date
2019-08-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
6
% buried
0
Peptide accession
P49023
Residue number A
564
Residue number B
585
Peptide name
Paxillin

Ligandability

Cysteine 564 of Paxillin

Cysteine 585 of Paxillin

A redox-regulated disulphide may form within Paxillin between cysteines 476 and 479 (63 and 66 respectively in this structure).

Details

Redox score ?
84
PDB code
7qb0
Structure name
solution structure of paxillin lim2/3
Structure deposition date
2021-11-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
7
% buried
11
Peptide accession
P49023
Residue number A
476
Residue number B
479
Peptide name
Paxillin

Ligandability

Cysteine 476 of Paxillin

Cysteine 479 of Paxillin

A redox-regulated disulphide may form within Paxillin between cysteines 561 and 585 (575 and 599 respectively in this structure).

Details

Redox score ?
83
PDB code
6u4n
Structure name
solution structure of paxillin lim4 in complex with kindlin-2 f0
Structure deposition date
2019-08-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
5
% buried
52
Peptide accession
P49023
Residue number A
561
Residue number B
585
Peptide name
Paxillin

Ligandability

Cysteine 561 of Paxillin

Cysteine 585 of Paxillin

A redox-regulated disulphide may form within Paxillin between cysteines 535 and 538 (549 and 552 respectively in this structure).

Details

Redox score ?
83
PDB code
6u4n
Structure name
solution structure of paxillin lim4 in complex with kindlin-2 f0
Structure deposition date
2019-08-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
0
Peptide accession
P49023
Residue number A
535
Residue number B
538
Peptide name
Paxillin

Ligandability

Cysteine 535 of Paxillin

Cysteine 538 of Paxillin

A redox-regulated disulphide may form within Paxillin between cysteines 561 and 582 (575 and 596 respectively in this structure).

Details

Redox score ?
82
PDB code
6u4m
Structure name
solution structure of paxillin lim4
Structure deposition date
2019-08-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
10
Peptide accession
P49023
Residue number A
561
Residue number B
582
Peptide name
Paxillin

Ligandability

Cysteine 561 of Paxillin

Cysteine 582 of Paxillin

A redox-regulated disulphide may form within Paxillin between cysteines 561 and 564 (575 and 578 respectively in this structure).

Details

Redox score ?
82
PDB code
6u4n
Structure name
solution structure of paxillin lim4 in complex with kindlin-2 f0
Structure deposition date
2019-08-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
5
% buried
46
Peptide accession
P49023
Residue number A
561
Residue number B
564
Peptide name
Paxillin

Ligandability

Cysteine 561 of Paxillin

Cysteine 564 of Paxillin

A redox-regulated disulphide may form within Paxillin between cysteines 476 and 499 (63 and 86 respectively in this structure).

Details

Redox score ?
79
PDB code
7qb0
Structure name
solution structure of paxillin lim2/3
Structure deposition date
2021-11-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
7
% buried
19
Peptide accession
P49023
Residue number A
476
Residue number B
499
Peptide name
Paxillin

Ligandability

Cysteine 476 of Paxillin

Cysteine 499 of Paxillin

A redox-regulated disulphide may form within Paxillin between cysteines 479 and 499 (66 and 86 respectively in this structure).

Details

Redox score ?
77
PDB code
7qb0
Structure name
solution structure of paxillin lim2/3
Structure deposition date
2021-11-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
9
Peptide accession
P49023
Residue number A
479
Residue number B
499
Peptide name
Paxillin

Ligandability

Cysteine 479 of Paxillin

Cysteine 499 of Paxillin

A redox-regulated disulphide may form within Paxillin between cysteines 446 and 464 (33 and 51 respectively in this structure).

Details

Redox score ?
77
PDB code
7qb0
Structure name
solution structure of paxillin lim2/3
Structure deposition date
2021-11-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
10
% buried
12
Peptide accession
P49023
Residue number A
446
Residue number B
464
Peptide name
Paxillin

Ligandability

Cysteine 446 of Paxillin

Cysteine 464 of Paxillin

A redox-regulated disulphide may form within Paxillin between cysteines 502 and 523 (89 and 110 respectively in this structure).

Details

Redox score ?
77
PDB code
7qb0
Structure name
solution structure of paxillin lim2/3
Structure deposition date
2021-11-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
18
Peptide accession
P49023
Residue number A
502
Residue number B
523
Peptide name
Paxillin

Ligandability

Cysteine 502 of Paxillin

Cysteine 523 of Paxillin

A redox-regulated disulphide may form within Paxillin between cysteines 564 and 582 (578 and 596 respectively in this structure).

Details

Redox score ?
73
PDB code
6u4n
Structure name
solution structure of paxillin lim4 in complex with kindlin-2 f0
Structure deposition date
2019-08-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
36
Peptide accession
P49023
Residue number A
564
Residue number B
582
Peptide name
Paxillin

Ligandability

Cysteine 564 of Paxillin

Cysteine 582 of Paxillin

A redox-regulated disulphide may form within Paxillin between cysteines 582 and 585 (596 and 599 respectively in this structure).

Details

Redox score ?
71
PDB code
6u4n
Structure name
solution structure of paxillin lim4 in complex with kindlin-2 f0
Structure deposition date
2019-08-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
42
Peptide accession
P49023
Residue number A
582
Residue number B
585
Peptide name
Paxillin

Ligandability

Cysteine 582 of Paxillin

Cysteine 585 of Paxillin

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