ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Poly(ADP-ribose) glycohydrolase

Intermolecular
Cysteine 599 and cysteine 599
Intramolecular
Cysteine 773 and cysteine 843
Cysteine 940 and cysteine 943 L
Cysteine 813 and cysteine 814
Cysteine 467 and cysteine 818
Cysteine 511 and cysteine 604
Cysteine 603 and cysteine 608
Cysteine 515 and cysteine 603
A redox-regulated disulphide may form between two units of Poly(ADP-ribose) glycohydrolase at cysteines 599 and 599. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
3uel
Structure name
crystal structure of the catalytic domain of rat poly (adp-ribose) glycohydrolase bound to adp-hpd
Structure deposition date
2011-10-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
60
Peptide A name
Poly(ADP-ribose) glycohydrolase
Peptide B name
Poly(ADP-ribose) glycohydrolase
Peptide A accession
Q9QYM2
Peptide B accession
Q9QYM2
Peptide A residue number
599
Peptide B residue number
599

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 Poly(ADP-ribose) glycohydrolase between cysteines 773 and 843.

Details

Redox score ?
71
PDB code
4na4
Structure name
crystal structure of mouse poly(adp-ribose) glycohydrolase (parg) catalytic domain with adp-hpd
Structure deposition date
2013-10-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
85
Minimum pKa ?
8
% buried
100
Peptide accession
O88622
Residue number A
773
Residue number B
843
Peptide name
Poly(ADP-ribose) glycohydrolase

Ligandability

Cysteine 773 of Poly(ADP-ribose) glycohydrolase

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 843 of Poly(ADP-ribose) glycohydrolase

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 Poly(ADP-ribose) glycohydrolase between cysteines 940 and 943.

Details

Redox score ?
65
PDB code
6hml
Structure name
polyadpribosyl glycosidase in complex with pdd00017299
Structure deposition date
2018-09-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
44
Minimum pKa ?
10
% buried
16
Peptide accession
Q86W56
Residue number A
940
Residue number B
943
Peptide name
Poly(ADP-ribose) glycohydrolase

Ligandability

Cysteine 940 of Poly(ADP-ribose) glycohydrolase

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 943 of Poly(ADP-ribose) glycohydrolase

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 Poly(ADP-ribose) glycohydrolase between cysteines 813 and 814. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3uel
Structure name
crystal structure of the catalytic domain of rat poly (adp-ribose) glycohydrolase bound to adp-hpd
Structure deposition date
2011-10-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
54
Peptide accession
Q9QYM2
Residue number A
813
Residue number B
814
Peptide name
Poly(ADP-ribose) glycohydrolase

Ligandability

Cysteine 813 of Poly(ADP-ribose) glycohydrolase

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 814 of Poly(ADP-ribose) glycohydrolase

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 Poly(ADP-ribose) glycohydrolase between cysteines 467 and 818. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
4a0d
Structure name
structure of unliganded human parg catalytic domain
Structure deposition date
2011-09-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
37
Peptide accession
Q86W56
Residue number A
467
Residue number B
818
Peptide name
Poly(ADP-ribose) glycohydrolase

Ligandability

Cysteine 467 of Poly(ADP-ribose) glycohydrolase

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 818 of Poly(ADP-ribose) glycohydrolase

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 Poly(ADP-ribose) glycohydrolase between cysteines 511 and 604. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
3uek
Structure name
crystal structure of the catalytic domain of rat poly (adp-ribose) glycohydrolase
Structure deposition date
2011-10-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
97
Peptide accession
Q9QYM2
Residue number A
511
Residue number B
604
Peptide name
Poly(ADP-ribose) glycohydrolase

Ligandability

Cysteine 511 of Poly(ADP-ribose) glycohydrolase

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 604 of Poly(ADP-ribose) glycohydrolase

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 Poly(ADP-ribose) glycohydrolase between cysteines 603 and 608. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
5a7r
Structure name
human poly(adp-ribose) glycohydrolase in complex with synthetic dimeric adp-ribose
Structure deposition date
2015-07-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
13
% buried
nan
Peptide accession
Q86W56
Residue number A
603
Residue number B
608
Peptide name
Poly(ADP-ribose) glycohydrolase

Ligandability

Cysteine 603 of Poly(ADP-ribose) glycohydrolase

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 608 of Poly(ADP-ribose) glycohydrolase

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 Poly(ADP-ribose) glycohydrolase between cysteines 515 and 603. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
5a7r
Structure name
human poly(adp-ribose) glycohydrolase in complex with synthetic dimeric adp-ribose
Structure deposition date
2015-07-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
13
% buried
nan
Peptide accession
Q86W56
Residue number A
515
Residue number B
603
Peptide name
Poly(ADP-ribose) glycohydrolase

Ligandability

Cysteine 515 of Poly(ADP-ribose) glycohydrolase

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 603 of Poly(ADP-ribose) glycohydrolase

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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