ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

Intermolecular
Cysteine 112 and cysteine 112
Cysteine 193 and cysteine 193
Cysteine 112 and cysteine 193
Intramolecular
Cysteine 59 and cysteine 75
Cysteine 244 and cysteine 265
Cysteine 92 and cysteine 172
Cysteine 152 and cysteine 165
Cysteine 92 and cysteine 152
Cysteine 152 and cysteine 172
Cysteine 165 and cysteine 172
Cysteine 92 and cysteine 165
A redox-regulated disulphide may form between two units of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase at cysteines 112 and 112.

Details

Redox score ?
64
PDB code
3gh3
Structure name
structural insights into the catalytic mechanism of cd38: evidence for a conformationally flexible covalent enzyme-substrate complex
Structure deposition date
2009-03-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide A name
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
Peptide B name
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
Peptide A accession
Q9TTF5
Peptide B accession
Q9TTF5
Peptide A residue number
112
Peptide B residue number
112

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 at cysteines 193 and 193.

Details

Redox score ?
63
PDB code
3ghh
Structure name
structural insights into the catalytic mechanism of cd38: evidence for a conformationally flexible covalent enzyme-substrate complex
Structure deposition date
2009-03-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide A name
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
Peptide B name
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
Peptide A accession
Q9TTF5
Peptide B accession
Q9TTF5
Peptide A residue number
193
Peptide B residue number
193

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 at cysteines 112 and 193.

Details

Redox score ?
62
PDB code
3gc6
Structure name
structural insights into the catalytic mechanism of cd38: evidence for a conformationally flexible covalent enzyme-substrate complex
Structure deposition date
2009-02-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide A name
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
Peptide B name
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
Peptide A accession
Q9TTF5
Peptide B accession
Q9TTF5
Peptide A residue number
112
Peptide B residue number
193

Ligandability

Cysteine 112 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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 193 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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 between cysteines 59 and 75.

Details

Redox score ?
86
PDB code
3p5s
Structure name
structural insights into the catalytic mechanism of cd38: evidence for a conformationally flexible covalent enzyme-substrate complex
Structure deposition date
2010-10-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9TTF5
Residue number A
59
Residue number B
75
Peptide name
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

Ligandability

Cysteine 59 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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 75 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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 between cysteines 244 and 265.

Details

Redox score ?
84
PDB code
3ghh
Structure name
structural insights into the catalytic mechanism of cd38: evidence for a conformationally flexible covalent enzyme-substrate complex
Structure deposition date
2009-03-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9TTF5
Residue number A
244
Residue number B
265
Peptide name
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

Ligandability

Cysteine 244 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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 265 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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 between cysteines 92 and 172.

Details

Redox score ?
83
PDB code
3kou
Structure name
structural insights into the catalytic mechanism of cd38: evidence for a conformationally flexible covalent enzyme-substrate complex
Structure deposition date
2009-11-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9TTF5
Residue number A
92
Residue number B
172
Peptide name
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

Ligandability

Cysteine 92 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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 between cysteines 152 and 165.

Details

Redox score ?
80
PDB code
3p5s
Structure name
structural insights into the catalytic mechanism of cd38: evidence for a conformationally flexible covalent enzyme-substrate complex
Structure deposition date
2010-10-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9TTF5
Residue number A
152
Residue number B
165
Peptide name
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

Ligandability

Cysteine 152 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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 165 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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 between cysteines 92 and 152. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
3gh3
Structure name
structural insights into the catalytic mechanism of cd38: evidence for a conformationally flexible covalent enzyme-substrate complex
Structure deposition date
2009-03-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9TTF5
Residue number A
92
Residue number B
152
Peptide name
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

Ligandability

Cysteine 92 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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 152 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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 between cysteines 152 and 172. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3gh3
Structure name
structural insights into the catalytic mechanism of cd38: evidence for a conformationally flexible covalent enzyme-substrate complex
Structure deposition date
2009-03-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9TTF5
Residue number A
152
Residue number B
172
Peptide name
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

Ligandability

Cysteine 152 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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 between cysteines 165 and 172. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3kou
Structure name
structural insights into the catalytic mechanism of cd38: evidence for a conformationally flexible covalent enzyme-substrate complex
Structure deposition date
2009-11-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9TTF5
Residue number A
165
Residue number B
172
Peptide name
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

Ligandability

Cysteine 165 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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 between cysteines 92 and 165. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3gh3
Structure name
structural insights into the catalytic mechanism of cd38: evidence for a conformationally flexible covalent enzyme-substrate complex
Structure deposition date
2009-03-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9TTF5
Residue number A
92
Residue number B
165
Peptide name
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

Ligandability

Cysteine 92 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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 165 of ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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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