ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Disintegrin and metalloproteinase domain-containing protein 17

Intramolecular
Cysteine 630 and cysteine 641
Cysteine 582 and cysteine 604
Cysteine 600 and cysteine 635
Cysteine 593 and cysteine 603
Cysteine 591 and cysteine 611
Cysteine 423 and cysteine 453
Cysteine 630 and cysteine 635
Cysteine 225 and cysteine 333
Cysteine 365 and cysteine 469
Cysteine 600 and cysteine 630
More...
Cysteine 635 and cysteine 641
Cysteine 593 and cysteine 611
Cysteine 600 and cysteine 641
Cysteine 591 and cysteine 593
Cysteine 591 and cysteine 603
Cysteine 603 and cysteine 611
Cysteine 333 and cysteine 365
Cysteine 333 and cysteine 469
Cysteine 225 and cysteine 469
Cysteine 582 and cysteine 591
Cysteine 582 and cysteine 603
Cysteine 591 and cysteine 604
Cysteine 225 and cysteine 365
Cysteine 603 and cysteine 604
Cysteine 582 and cysteine 611
Cysteine 582 and cysteine 593
Cysteine 593 and cysteine 604
Cysteine 604 and cysteine 611
Cysteine 593 and cysteine 630
Cysteine 603 and cysteine 635
Cysteine 593 and cysteine 635
Cysteine 603 and cysteine 641
Cysteine 593 and cysteine 641
Cysteine 603 and cysteine 630
Cysteine 600 and cysteine 603
Cysteine 593 and cysteine 600
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 630 and 641 (50 and 61 respectively in this structure).

Details

Redox score ?
89
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
630
Residue number B
641
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 630 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 641 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 582 and 604 (2 and 24 respectively in this structure).

Details

Redox score ?
87
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
582
Residue number B
604
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 582 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 604 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 600 and 635 (20 and 55 respectively in this structure).

Details

Redox score ?
85
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
600
Residue number B
635
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 600 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 635 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 593 and 603 (13 and 23 respectively in this structure).

Details

Redox score ?
83
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
593
Residue number B
603
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 593 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 603 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 591 and 611 (11 and 31 respectively in this structure).

Details

Redox score ?
82
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
591
Residue number B
611
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 591 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 611 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 423 and 453.

Details

Redox score ?
82
PDB code
2ddf
Structure name
crystal structure of tace in complex with tapi-2
Structure deposition date
2006-01-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
423
Residue number B
453
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 423 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 453 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 630 and 635 (50 and 55 respectively in this structure).

Details

Redox score ?
81
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
630
Residue number B
635
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 630 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 635 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 225 and 333.

Details

Redox score ?
78
PDB code
3lea
Structure name
crystal structure of the catalytic domain of tace with isoindolinone- biphenyl-hydantoin inhibitor
Structure deposition date
2010-01-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
225
Residue number B
333
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 225 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 333 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 365 and 469.

Details

Redox score ?
78
PDB code
2i47
Structure name
crystal structure of catalytic domain of tace with inhibitor
Structure deposition date
2006-08-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
365
Residue number B
469
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 365 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 469 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 600 and 630 (20 and 50 respectively in this structure).

Details

Redox score ?
74
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
600
Residue number B
630
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 600 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 630 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 635 and 641 (55 and 61 respectively in this structure).

Details

Redox score ?
74
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
635
Residue number B
641
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 635 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 641 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 593 and 611 (13 and 31 respectively in this structure).

Details

Redox score ?
70
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
593
Residue number B
611
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 593 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 611 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 600 and 641 (20 and 61 respectively in this structure).

Details

Redox score ?
68
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
600
Residue number B
641
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 600 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 641 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 591 and 593 (11 and 13 respectively in this structure).

Details

Redox score ?
66
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
591
Residue number B
593
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 591 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 593 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 591 and 603 (11 and 23 respectively in this structure).

Details

Redox score ?
64
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
591
Residue number B
603
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 591 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 603 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 603 and 611 (23 and 31 respectively in this structure).

Details

Redox score ?
63
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
603
Residue number B
611
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 603 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 611 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 333 and 365.

Details

Redox score ?
62
PDB code
3le9
Structure name
crystal structure of the catalytic domain of tace with indazolinone- phenyl-hydantoin inhibitor
Structure deposition date
2010-01-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
333
Residue number B
365
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 333 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 365 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 333 and 469.

Details

Redox score ?
61
PDB code
3b92
Structure name
novel thio-based tace inhibitors part 2: rational design, synthesis and sar of thiol-contaning aryl sufones
Structure deposition date
2007-11-02
Thiol separation (Å)
3
Half-sphere exposure sum ?
73
Minimum pKa ?
14
% buried
92
Peptide accession
P78536
Residue number A
333
Residue number B
469
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 333 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 469 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 225 and 469.

Details

Redox score ?
60
PDB code
3o64
Structure name
crystal structure of catalytic domain of tace with 2-(2-aminothiazol- 4-yl)pyrrolidine-based tartrate diamides
Structure deposition date
2010-07-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
225
Residue number B
469
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 225 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 469 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 582 and 591 (2 and 11 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
582
Residue number B
591
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 582 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 591 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 582 and 603 (2 and 23 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
582
Residue number B
603
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 582 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 603 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 591 and 604 (11 and 24 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
591
Residue number B
604
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 591 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 604 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 225 and 365. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
3kme
Structure name
crystal structure of catalytic domain of tace with phenyl- pyrrolidinyl-tartrate inhibitor
Structure deposition date
2009-11-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
225
Residue number B
365
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 225 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 365 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 603 and 604 (23 and 24 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
603
Residue number B
604
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 603 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 604 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 582 and 611 (2 and 31 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
582
Residue number B
611
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 582 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 611 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 582 and 593 (2 and 13 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
582
Residue number B
593
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 582 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 593 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 593 and 604 (13 and 24 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
593
Residue number B
604
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 593 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 604 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 604 and 611 (24 and 31 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
604
Residue number B
611
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 604 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 611 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 593 and 630 (13 and 50 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
593
Residue number B
630
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 593 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 630 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 603 and 635 (23 and 55 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
603
Residue number B
635
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 603 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 635 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 593 and 635 (13 and 55 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
593
Residue number B
635
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 593 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 635 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 603 and 641 (23 and 61 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
603
Residue number B
641
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 603 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 641 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 593 and 641 (13 and 61 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
593
Residue number B
641
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 593 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 641 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 603 and 630 (23 and 50 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
603
Residue number B
630
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 603 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 630 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 600 and 603 (20 and 23 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
600
Residue number B
603
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 600 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 603 of Disintegrin and metalloproteinase domain-containing protein 17

A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 17 between cysteines 593 and 600 (13 and 20 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2m2f
Structure name
the membran-proximal domain of adam17
Structure deposition date
2012-12-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P78536
Residue number A
593
Residue number B
600
Peptide name
Disintegrin and metalloproteinase domain-containing protein 17

Ligandability

Cysteine 593 of Disintegrin and metalloproteinase domain-containing protein 17

Cysteine 600 of Disintegrin and metalloproteinase domain-containing protein 17

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