a tool for identifying drug-targetable redox-active disulphides

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Intermolecular

Cysteine 119 and cysteine 119

Cysteine 201 and cysteine 119

Cysteine 201 and cysteine 201

Intramolecular

Cysteine 67 and cysteine 82

Cysteine 254 and cysteine 275 L

Cysteine 258 and cysteine 279 L

Cysteine 99 and cysteine 180

Cysteine 160 and cysteine 173

Cysteine 287 and cysteine 296 L

Cysteine 99 and cysteine 160

Cysteine 173 and cysteine 180

Cysteine 99 and cysteine 173

Cysteine 160 and cysteine 180

A redox-regulated disulphide may form between two units of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 at cysteines 119 and 119.

Details

Redox score ?

72

PDB code

Structure name

dynamic conformations of the cd38-mediated nad cyclization captured using multi-copy crystallography

Structure deposition date

2010-08-16

Thiol separation (Å)

3

Half-sphere exposure sum ?

86

Minimum pK_a ?

nan

% buried

nan

Peptide A name

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Peptide B name

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Peptide A accession

Peptide B accession

Peptide A residue number

119

Peptide B residue number

119

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 two units of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 at cysteines 201 and 119.

Details

Redox score ?

69

PDB code

Structure name

dynamic conformations of the cd38-mediated nad cyclization captured using multi-copy crystallography

Structure deposition date

2010-08-16

Thiol separation (Å)

4

Half-sphere exposure sum ?

83

Minimum pK_a ?

nan

% buried

nan

Peptide A name

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Peptide B name

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Peptide A accession

Peptide B accession

Peptide A residue number

201

Peptide B residue number

119

Ligandability

Cysteine 201 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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 119 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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 between two units of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 at cysteines 201 and 201.

Details

Redox score ?

60

PDB code

Structure name

dynamic conformations of the cd38-mediated nad cyclization captured using multi-copy crystallography

Structure deposition date

2010-08-16

Thiol separation (Å)

5

Half-sphere exposure sum ?

77

Minimum pK_a ?

nan

% buried

nan

Peptide A name

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Peptide B name

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Peptide A accession

Peptide B accession

Peptide A residue number

201

Peptide B residue number

201

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 within ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 between cysteines 67 and 82.

Details

Redox score ?

86

PDB code

Structure name

crystal structure of the extracellular domain of human cd38

Structure deposition date

2007-02-20

Thiol separation (Å)

2

Half-sphere exposure sum ?

66

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

67

Residue number B

82

Peptide name

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Ligandability

Cysteine 67 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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 82 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 between cysteines 254 and 275.

Details

Redox score ?

86

PDB code

Structure name

acidic residues at the active sites of cd38 and adp-ribosyl cyclase determine naapd synthesis and hydrolysis activities

Structure deposition date

2006-06-18

Thiol separation (Å)

2

Half-sphere exposure sum ?

58

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

254

Residue number B

275

Peptide name

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Ligandability

Cysteine 254 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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 275 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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.

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 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 between cysteines 258 and 279.

Details

Redox score ?

85

PDB code

Structure name

crystal structure of the truncated extracellular domain of mouse cd38

Structure deposition date

2007-02-28

Thiol separation (Å)

2

Half-sphere exposure sum ?

65

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

258

Residue number B

279

Peptide name

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Ligandability

Cysteine 258 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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 279 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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.

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 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 between cysteines 99 and 180.

Details

Redox score ?

82

PDB code

Structure name

crystal structure of the extracellular domain of human cd38

Structure deposition date

2007-02-20

Thiol separation (Å)

2

Half-sphere exposure sum ?

52

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

99

Residue number B

180

Peptide name

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Ligandability

Cysteine 99 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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 180 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 between cysteines 160 and 173.

Details

Redox score ?

81

PDB code

Structure name

crystal structure of human cd38 in complex with the fab fragment of antibody hb7

Structure deposition date

2011-03-28

Thiol separation (Å)

2

Half-sphere exposure sum ?

79

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

160

Residue number B

173

Peptide name

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Ligandability

Cysteine 160 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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 173 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 between cysteines 287 and 296 (243 and 252 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 cd38 in complex with daratumumab

Structure deposition date

2020-11-13

Thiol separation (Å)

9

Half-sphere exposure sum ?

55

Minimum pK_a ?

10

% buried

54

Peptide accession

Residue number A

287

Residue number B

296

Peptide name

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Ligandability

Cysteine 287 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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.

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 296 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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.

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 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 between cysteines 99 and 160. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

39

PDB code

Structure name

crystal structure of the extracellular domain of human cd38

Structure deposition date

2007-02-20

Thiol separation (Å)

9

Half-sphere exposure sum ?

76

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

99

Residue number B

160

Peptide name

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Ligandability

Cysteine 99 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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 160 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 between cysteines 173 and 180. 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 human cd38 extracellular domain complexed with a covalent intermediate, ara-f-ribose-5'-phosphate

Structure deposition date

2008-07-29

Thiol separation (Å)

10

Half-sphere exposure sum ?

59

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

173

Residue number B

180

Peptide name

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Ligandability

Cysteine 173 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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 180 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 between cysteines 99 and 173. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

37

PDB code

Structure name

crystal structure of human cd38 extracellular domain, gtp complex

Structure deposition date

2008-07-29

Thiol separation (Å)

10

Half-sphere exposure sum ?

64

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

99

Residue number B

173

Peptide name

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Ligandability

Cysteine 99 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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 173 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 between cysteines 160 and 180 (116 and 136 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

37

PDB code

Structure name

crystal structure of daratumumab fab and cd38 complex

Structure deposition date

2021-01-10

Thiol separation (Å)

10

Half-sphere exposure sum ?

59

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

160

Residue number B

180

Peptide name

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Ligandability

Cysteine 160 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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 180 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 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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