ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Protein mono-ADP-ribosyltransferase PARP14

Intermolecular
Cysteine 1618 and cysteine 1618
Intramolecular
Cysteine 1265 and cysteine 1295
Cysteine 1295 and cysteine 1327
A redox-regulated disulphide may form between two units of Protein mono-ADP-ribosyltransferase PARP14 at cysteines 1618 and 1618. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
7lun
Structure name
human parp14 (artd8), catalytic fragment in complex with rbn011980
Structure deposition date
2021-02-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
48
Minimum pKa ?
10
% buried
56
Peptide A name
Protein mono-ADP-ribosyltransferase PARP14
Peptide B name
Protein mono-ADP-ribosyltransferase PARP14
Peptide A accession
Q460N5
Peptide B accession
Q460N5
Peptide A residue number
1618
Peptide B residue number
1618

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 Protein mono-ADP-ribosyltransferase PARP14 between cysteines 1265 and 1295. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
5qht
Structure name
pandda analysis group deposition -- crystal structure of human parp14 macrodomain 3 in complex with fmopl000065a
Structure deposition date
2019-03-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
36
Peptide accession
Q460N5
Residue number A
1265
Residue number B
1295
Peptide name
Protein mono-ADP-ribosyltransferase PARP14

Ligandability

Cysteine 1265 of Protein mono-ADP-ribosyltransferase PARP14

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 1295 of Protein mono-ADP-ribosyltransferase PARP14

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 Protein mono-ADP-ribosyltransferase PARP14 between cysteines 1295 and 1327. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
5qi5
Structure name
pandda analysis group deposition of models with modelled events (e
Structure deposition date
2018-05-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
72
Peptide accession
Q460N5
Residue number A
1295
Residue number B
1327
Peptide name
Protein mono-ADP-ribosyltransferase PARP14

Ligandability

Cysteine 1295 of Protein mono-ADP-ribosyltransferase PARP14

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 1327 of Protein mono-ADP-ribosyltransferase PARP14

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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