a tool for identifying drug-targetable redox-active disulphides

LHFPL tetraspan subfamily member 5 protein

Intermolecular

Cysteine 35 and cysteine 35

Cysteine 1392 of Protocadherin-15 and cysteine 35

Intramolecular

Cysteine 68 and cysteine 79

Cysteine 114 and cysteine 130

Cysteine 121 and cysteine 130

Cysteine 114 and cysteine 121

A redox-regulated disulphide may form between two units of LHFPL tetraspan subfamily member 5 protein at cysteines 35 and 35.

Details

Redox score ?

64

PDB code

Structure name

cryoem structure of mouse pcdh15-1ec-lhfpl5 complex

Structure deposition date

2018-01-03

Thiol separation (Å)

5

Half-sphere exposure sum ?

76

Minimum pK_a ?

8

% buried

96

Peptide A name

LHFPL tetraspan subfamily member 5 protein

Peptide B name

LHFPL tetraspan subfamily member 5 protein

Peptide A accession

Peptide B accession

Peptide A residue number

35

Peptide B residue number

35

Ligandability

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 between cysteine 1392 of Protocadherin-15 and cysteine 35 of LHFPL tetraspan subfamily member 5 protein. 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

cryoem structure of mouse pcdh15-1ec-lhfpl5 complex

Structure deposition date

2018-01-03

Thiol separation (Å)

7

Half-sphere exposure sum ?

68

Minimum pK_a ?

11

% buried

81

Peptide A name

Protocadherin-15

Peptide B name

LHFPL tetraspan subfamily member 5 protein

Peptide A accession

Peptide B accession

Peptide A residue number

1392

Peptide B residue number

35

Ligandability

Cysteine 1392 of Protocadherin-15

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 35 of LHFPL tetraspan subfamily member 5 protein

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 LHFPL tetraspan subfamily member 5 protein between cysteines 68 and 79.

Details

Redox score ?

84

PDB code

Structure name

cryoem structure of mouse pcdh15-1ec-lhfpl5 complex

Structure deposition date

2018-01-03

Thiol separation (Å)

2

Half-sphere exposure sum ?

50

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

68

Residue number B

79

Peptide name

LHFPL tetraspan subfamily member 5 protein

Ligandability

Cysteine 68 of LHFPL tetraspan subfamily member 5 protein

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 79 of LHFPL tetraspan subfamily member 5 protein

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 LHFPL tetraspan subfamily member 5 protein between cysteines 114 and 130.

Details

Redox score ?

82

PDB code

Structure name

cryoem structure of mouse pcdh15-1ec-lhfpl5 complex

Structure deposition date

2018-01-03

Thiol separation (Å)

2

Half-sphere exposure sum ?

70

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

114

Residue number B

130

Peptide name

LHFPL tetraspan subfamily member 5 protein

Ligandability

Cysteine 114 of LHFPL tetraspan subfamily member 5 protein

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 130 of LHFPL tetraspan subfamily member 5 protein

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 LHFPL tetraspan subfamily member 5 protein between cysteines 121 and 130. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

46

PDB code

Structure name

cryoem structure of mouse pcdh15-1ec-lhfpl5 complex

Structure deposition date

2018-01-03

Thiol separation (Å)

9

Half-sphere exposure sum ?

53

Minimum pK_a ?

9

% buried

nan

Peptide accession

Residue number A

121

Residue number B

130

Peptide name

LHFPL tetraspan subfamily member 5 protein

Ligandability

Cysteine 121 of LHFPL tetraspan subfamily member 5 protein

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 130 of LHFPL tetraspan subfamily member 5 protein

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 LHFPL tetraspan subfamily member 5 protein between cysteines 114 and 121. 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

cryoem structure of mouse pcdh15-1ec-lhfpl5 complex

Structure deposition date

2018-01-03

Thiol separation (Å)

9

Half-sphere exposure sum ?

46

Minimum pK_a ?

9

% buried

nan

Peptide accession

Residue number A

114

Residue number B

121

Peptide name

LHFPL tetraspan subfamily member 5 protein

Ligandability

Cysteine 114 of LHFPL tetraspan subfamily member 5 protein

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 121 of LHFPL tetraspan subfamily member 5 protein

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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