a tool for identifying drug-targetable redox-active disulphides

Alpha-galactosidase A

Intramolecular

Cysteine 378 and cysteine 382

Cysteine 52 and cysteine 94 L

Cysteine 142 and cysteine 172

Cysteine 202 and cysteine 223 L

Cysteine 56 and cysteine 63 L

Cysteine 172 and cysteine 174

Cysteine 142 and cysteine 174

Cysteine 94 and cysteine 142

A redox-regulated disulphide may form within Alpha-galactosidase A between cysteines 378 and 382.

Details

Redox score ?

83

PDB code

Structure name

human alpha-galactosidase catalytic mechanism 4

Structure deposition date

2009-05-13

Thiol separation (Å)

2

Half-sphere exposure sum ?

72

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

378

Residue number B

382

Peptide name

Alpha-galactosidase A

Ligandability

Cysteine 378 of Alpha-galactosidase A

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 Alpha-galactosidase A

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 Alpha-galactosidase A between cysteines 52 and 94.

Details

Redox score ?

81

PDB code

Structure name

pharmacological chaperoning in human alpha-galactosidase

Structure deposition date

2011-09-19

Thiol separation (Å)

2

Half-sphere exposure sum ?

64

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

52

Residue number B

94

Peptide name

Alpha-galactosidase A

Ligandability

Cysteine 52 of Alpha-galactosidase A

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 94 of Alpha-galactosidase A

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 Alpha-galactosidase A between cysteines 142 and 172.

Details

Redox score ?

78

PDB code

Structure name

pharmacological chaperoning in human alpha-galactosidase

Structure deposition date

2011-05-23

Thiol separation (Å)

2

Half-sphere exposure sum ?

60

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

142

Residue number B

172

Peptide name

Alpha-galactosidase A

Ligandability

Cysteine 142 of Alpha-galactosidase A

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 172 of Alpha-galactosidase A

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 Alpha-galactosidase A between cysteines 202 and 223.

Details

Redox score ?

77

PDB code

Structure name

human alpha-galactosidase catalytic mechanism 1

Structure deposition date

2009-05-13

Thiol separation (Å)

2

Half-sphere exposure sum ?

92

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

202

Residue number B

223

Peptide name

Alpha-galactosidase A

Ligandability

Cysteine 202 of Alpha-galactosidase A

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 223 of Alpha-galactosidase A

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Alpha-galactosidase A between cysteines 56 and 63.

Details

Redox score ?

74

PDB code

Structure name

pharmacological chaperoning in human alpha-galactosidase

Structure deposition date

2011-05-23

Thiol separation (Å)

5

Half-sphere exposure sum ?

49

Minimum pK_a ?

nan

% buried

10

Peptide accession

Residue number A

56

Residue number B

63

Peptide name

Alpha-galactosidase A

Ligandability

Cysteine 56 of Alpha-galactosidase A

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 63 of Alpha-galactosidase A

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Alpha-galactosidase A between cysteines 172 and 174. 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 human alpha-galactosidase

Structure deposition date

2003-10-03

Thiol separation (Å)

9

Half-sphere exposure sum ?

60

Minimum pK_a ?

11

% buried

nan

Peptide accession

Residue number A

172

Residue number B

174

Peptide name

Alpha-galactosidase A

Ligandability

Cysteine 172 of Alpha-galactosidase A

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 174 of Alpha-galactosidase A

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 Alpha-galactosidase A between cysteines 142 and 174. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

38

PDB code

Structure name

structure of human alpha-galactosidase

Structure deposition date

2003-10-03

Thiol separation (Å)

10

Half-sphere exposure sum ?

52

Minimum pK_a ?

11

% buried

nan

Peptide accession

Residue number A

142

Residue number B

174

Peptide name

Alpha-galactosidase A

Ligandability

Cysteine 142 of Alpha-galactosidase A

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 174 of Alpha-galactosidase A

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 Alpha-galactosidase A between cysteines 94 and 142. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

38

PDB code

Structure name

crystal structure of apo alpha-galactosidase a at ph 4

Structure deposition date

2009-04-02

Thiol separation (Å)

9

Half-sphere exposure sum ?

65

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

94

Residue number B

142

Peptide name

Alpha-galactosidase A

Ligandability

Cysteine 94 of Alpha-galactosidase A

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 142 of Alpha-galactosidase A

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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