a tool for identifying drug-targetable redox-active disulphides

Carboxypeptidase M

Intramolecular

Cysteine 341 and cysteine 410

Cysteine 242 and cysteine 284

Cysteine 138 and cysteine 285

Cysteine 138 and cysteine 284

Cysteine 284 and cysteine 285

Cysteine 242 and cysteine 285

A redox-regulated disulphide may form within Carboxypeptidase M between cysteines 341 and 410 (324 and 393 respectively in this structure).

Details

Redox score ?

87

PDB code

Structure name

crystal structure of human carboxypeptidase m

Structure deposition date

2004-02-17

Thiol separation (Å)

2

Half-sphere exposure sum ?

49

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

341

Residue number B

410

Peptide name

Carboxypeptidase M

Ligandability

Cysteine 341 of Carboxypeptidase M

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 410 of Carboxypeptidase M

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 Carboxypeptidase M between cysteines 242 and 284 (225 and 267 respectively in this structure).

Details

Redox score ?

86

PDB code

Structure name

crystal structure of human carboxypeptidase m

Structure deposition date

2004-02-17

Thiol separation (Å)

2

Half-sphere exposure sum ?

57

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

242

Residue number B

284

Peptide name

Carboxypeptidase M

Ligandability

Cysteine 242 of Carboxypeptidase M

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 284 of Carboxypeptidase M

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 Carboxypeptidase M between cysteines 138 and 285 (121 and 268 respectively in this structure).

Details

Redox score ?

83

PDB code

Structure name

crystal structure of human carboxypeptidase m

Structure deposition date

2004-02-17

Thiol separation (Å)

2

Half-sphere exposure sum ?

56

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

138

Residue number B

285

Peptide name

Carboxypeptidase M

Ligandability

Cysteine 138 of Carboxypeptidase M

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 285 of Carboxypeptidase M

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 Carboxypeptidase M between cysteines 138 and 284 (121 and 267 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

Structure name

crystal structure of human carboxypeptidase m

Structure deposition date

2004-02-17

Thiol separation (Å)

9

Half-sphere exposure sum ?

56

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

138

Residue number B

284

Peptide name

Carboxypeptidase M

Ligandability

Cysteine 138 of Carboxypeptidase M

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 284 of Carboxypeptidase M

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 Carboxypeptidase M between cysteines 284 and 285 (267 and 268 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

44

PDB code

Structure name

crystal structure of human carboxypeptidase m

Structure deposition date

2004-02-17

Thiol separation (Å)

8

Half-sphere exposure sum ?

63

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

284

Residue number B

285

Peptide name

Carboxypeptidase M

Ligandability

Cysteine 284 of Carboxypeptidase M

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 285 of Carboxypeptidase M

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 Carboxypeptidase M between cysteines 242 and 285 (225 and 268 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

Structure name

crystal structure of human carboxypeptidase m

Structure deposition date

2004-02-17

Thiol separation (Å)

10

Half-sphere exposure sum ?

57

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

242

Residue number B

285

Peptide name

Carboxypeptidase M

Ligandability

Cysteine 242 of Carboxypeptidase M

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 285 of Carboxypeptidase M

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.

If this tool was useful for finding a disulphide, please cite: