a tool for identifying drug-targetable redox-active disulphides

Brefeldin A-inhibited guanine nucleotide-exchange protein 1

Intramolecular

Cysteine 88 and cysteine 137

Cysteine 135 and cysteine 178

Cysteine 135 and cysteine 137

Cysteine 88 and cysteine 102

A redox-regulated disulphide may form within Brefeldin A-inhibited guanine nucleotide-exchange protein 1 between cysteines 88 and 137.

Details

Redox score ?

75

PDB code

Structure name

crystal structure of arl1-gtp and dcb domain of big1 complex

Structure deposition date

2016-04-02

Thiol separation (Å)

4

Half-sphere exposure sum ?

79

Minimum pK_a ?

7

% buried

74

Peptide accession

Residue number A

88

Residue number B

137

Peptide name

Brefeldin A-inhibited guanine nucleotide-exchange protein 1

Ligandability

Cysteine 88 of Brefeldin A-inhibited guanine nucleotide-exchange protein 1

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 137 of Brefeldin A-inhibited guanine nucleotide-exchange protein 1

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 Brefeldin A-inhibited guanine nucleotide-exchange protein 1 between cysteines 135 and 178. 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

structure of human arl1 in complex with the dcb domain of big1

Structure deposition date

2015-10-22

Thiol separation (Å)

7

Half-sphere exposure sum ?

82

Minimum pK_a ?

11

% buried

90

Peptide accession

Residue number A

135

Residue number B

178

Peptide name

Brefeldin A-inhibited guanine nucleotide-exchange protein 1

Ligandability

Cysteine 135 of Brefeldin A-inhibited guanine nucleotide-exchange protein 1

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 178 of Brefeldin A-inhibited guanine nucleotide-exchange protein 1

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 Brefeldin A-inhibited guanine nucleotide-exchange protein 1 between cysteines 135 and 137. 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 arl1-gtp and dcb domain of big1 complex

Structure deposition date

2016-04-02

Thiol separation (Å)

9

Half-sphere exposure sum ?

84

Minimum pK_a ?

11

% buried

72

Peptide accession

Residue number A

135

Residue number B

137

Peptide name

Brefeldin A-inhibited guanine nucleotide-exchange protein 1

Ligandability

Cysteine 135 of Brefeldin A-inhibited guanine nucleotide-exchange protein 1

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 137 of Brefeldin A-inhibited guanine nucleotide-exchange protein 1

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 Brefeldin A-inhibited guanine nucleotide-exchange protein 1 between cysteines 88 and 102. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

35

PDB code

Structure name

structure of human arl1 in complex with the dcb domain of big1

Structure deposition date

2015-10-22

Thiol separation (Å)

10

Half-sphere exposure sum ?

79

Minimum pK_a ?

8

% buried

98

Peptide accession

Residue number A

88

Residue number B

102

Peptide name

Brefeldin A-inhibited guanine nucleotide-exchange protein 1

Ligandability

Cysteine 88 of Brefeldin A-inhibited guanine nucleotide-exchange protein 1

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 102 of Brefeldin A-inhibited guanine nucleotide-exchange protein 1

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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