a tool for identifying drug-targetable redox-active disulphides

Dipeptidyl peptidase 2

Intramolecular

Cysteine 332 and cysteine 338

Cysteine 246 and cysteine 322

Cysteine 352 and cysteine 382

Cysteine 216 and cysteine 293

Cysteine 338 and cysteine 352

Cysteine 332 and cysteine 352

Cysteine 332 and cysteine 382

Cysteine 338 and cysteine 382

A redox-regulated disulphide may form within Dipeptidyl peptidase 2 between cysteines 332 and 338.

Details

Redox score ?

85

PDB code

Structure name

structure of dpp2

Structure deposition date

2012-03-23

Thiol separation (Å)

2

Half-sphere exposure sum ?

64

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

332

Residue number B

338

Peptide name

Dipeptidyl peptidase 2

Ligandability

Cysteine 332 of Dipeptidyl peptidase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 338 of Dipeptidyl peptidase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dipeptidyl peptidase 2 between cysteines 246 and 322.

Details

Redox score ?

84

PDB code

Structure name

structure of dpp2

Structure deposition date

2012-03-23

Thiol separation (Å)

2

Half-sphere exposure sum ?

46

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

246

Residue number B

322

Peptide name

Dipeptidyl peptidase 2

Ligandability

Cysteine 246 of Dipeptidyl peptidase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 322 of Dipeptidyl peptidase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dipeptidyl peptidase 2 between cysteines 352 and 382.

Details

Redox score ?

82

PDB code

Structure name

human dipeptidil peptidase dpp7 complexed with inhibitor gsk237826a

Structure deposition date

2010-05-14

Thiol separation (Å)

2

Half-sphere exposure sum ?

76

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

352

Residue number B

382

Peptide name

Dipeptidyl peptidase 2

Ligandability

Cysteine 352 of Dipeptidyl peptidase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 382 of Dipeptidyl peptidase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dipeptidyl peptidase 2 between cysteines 216 and 293.

Details

Redox score ?

82

PDB code

Structure name

structure of dpp2

Structure deposition date

2012-03-23

Thiol separation (Å)

2

Half-sphere exposure sum ?

69

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

216

Residue number B

293

Peptide name

Dipeptidyl peptidase 2

Ligandability

Cysteine 216 of Dipeptidyl peptidase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 293 of Dipeptidyl peptidase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dipeptidyl peptidase 2 between cysteines 338 and 352. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

47

PDB code

Structure name

structure of dpp2

Structure deposition date

2012-03-23

Thiol separation (Å)

8

Half-sphere exposure sum ?

70

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

338

Residue number B

352

Peptide name

Dipeptidyl peptidase 2

Ligandability

Cysteine 338 of Dipeptidyl peptidase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 352 of Dipeptidyl peptidase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dipeptidyl peptidase 2 between cysteines 332 and 352. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

45

PDB code

Structure name

structure of dpp2

Structure deposition date

2012-03-23

Thiol separation (Å)

8

Half-sphere exposure sum ?

74

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

332

Residue number B

352

Peptide name

Dipeptidyl peptidase 2

Ligandability

Cysteine 332 of Dipeptidyl peptidase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 352 of Dipeptidyl peptidase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dipeptidyl peptidase 2 between cysteines 332 and 382. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

43

PDB code

Structure name

human dipeptidyl peptidase dpp7

Structure deposition date

2009-09-21

Thiol separation (Å)

9

Half-sphere exposure sum ?

67

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

332

Residue number B

382

Peptide name

Dipeptidyl peptidase 2

Ligandability

Cysteine 332 of Dipeptidyl peptidase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 382 of Dipeptidyl peptidase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Dipeptidyl peptidase 2 between cysteines 338 and 382. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

42

PDB code

Structure name

structure of dpp2

Structure deposition date

2012-03-23

Thiol separation (Å)

10

Half-sphere exposure sum ?

59

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

338

Residue number B

382

Peptide name

Dipeptidyl peptidase 2

Ligandability

Cysteine 338 of Dipeptidyl peptidase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 382 of Dipeptidyl peptidase 2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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