ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Histone PARylation factor 1

Intramolecular
Cysteine 152 and cysteine 299 L
Cysteine 152 and cysteine 252 L
Cysteine 252 and cysteine 299
A redox-regulated disulphide may form within Histone PARylation factor 1 between cysteines 152 and 299.

Details

Redox score ?
70
PDB code
6tx3
Structure name
hpf1 bound to catalytic fragment of parp2
Structure deposition date
2020-01-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
84
Peptide accession
Q9NWY4
Residue number A
152
Residue number B
299
Peptide name
Histone PARylation factor 1

Ligandability

Cysteine 152 of Histone PARylation factor 1

Not ligandable in the dataset of Yang et al.

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 299 of Histone PARylation factor 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 Histone PARylation factor 1 between cysteines 152 and 252. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6x0m
Structure name
bridging of double-strand dna break activates parp2/hpf1 to modify chromatin
Structure deposition date
2020-05-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
7
% buried
68
Peptide accession
Q9NWY4
Residue number A
152
Residue number B
252
Peptide name
Histone PARylation factor 1

Ligandability

Cysteine 152 of Histone PARylation factor 1

Not ligandable in the dataset of Yang et al.

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 252 of Histone PARylation factor 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 Histone PARylation factor 1 between cysteines 252 and 299. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
6x0m
Structure name
bridging of double-strand dna break activates parp2/hpf1 to modify chromatin
Structure deposition date
2020-05-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
12
% buried
86
Peptide accession
Q9NWY4
Residue number A
252
Residue number B
299
Peptide name
Histone PARylation factor 1

Ligandability

Cysteine 252 of Histone PARylation factor 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 299 of Histone PARylation factor 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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