ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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DNA repair protein RAD50

Intermolecular
Cysteine 684 and cysteine 684
Cysteine 681 and cysteine 681
Intramolecular
Cysteine 681 and cysteine 684
Cysteine 680 and cysteine 681
Cysteine 680 and cysteine 684
A redox-regulated disulphide may form between two units of DNA repair protein RAD50 at cysteines 684 and 684.

Details

Redox score ?
85
PDB code
5gox
Structure name
eukaryotic rad50 functions as a rod-shaped dimer
Structure deposition date
2016-07-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
5
% buried
nan
Peptide A name
DNA repair protein RAD50
Peptide B name
DNA repair protein RAD50
Peptide A accession
Q92878
Peptide B accession
Q92878
Peptide A residue number
684
Peptide B residue number
684

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 DNA repair protein RAD50 at cysteines 681 and 681.

Details

Redox score ?
63
PDB code
5gox
Structure name
eukaryotic rad50 functions as a rod-shaped dimer
Structure deposition date
2016-07-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
13
% buried
83
Peptide A name
DNA repair protein RAD50
Peptide B name
DNA repair protein RAD50
Peptide A accession
Q92878
Peptide B accession
Q92878
Peptide A residue number
681
Peptide B residue number
681

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 DNA repair protein RAD50 between cysteines 681 and 684.

Details

Redox score ?
84
PDB code
5gox
Structure name
eukaryotic rad50 functions as a rod-shaped dimer
Structure deposition date
2016-07-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
65
Minimum pKa ?
5
% buried
72
Peptide accession
Q92878
Residue number A
681
Residue number B
684
Peptide name
DNA repair protein RAD50

Ligandability

Cysteine 681 of DNA repair protein RAD50

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 684 of DNA repair protein RAD50

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 DNA repair protein RAD50 between cysteines 680 and 681. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
5gox
Structure name
eukaryotic rad50 functions as a rod-shaped dimer
Structure deposition date
2016-07-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
52
Peptide accession
Q92878
Residue number A
680
Residue number B
681
Peptide name
DNA repair protein RAD50

Ligandability

Cysteine 680 of DNA repair protein RAD50

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 681 of DNA repair protein RAD50

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 DNA repair protein RAD50 between cysteines 680 and 684. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
5gox
Structure name
eukaryotic rad50 functions as a rod-shaped dimer
Structure deposition date
2016-07-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
nan
Peptide accession
Q92878
Residue number A
680
Residue number B
684
Peptide name
DNA repair protein RAD50

Ligandability

Cysteine 680 of DNA repair protein RAD50

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 684 of DNA repair protein RAD50

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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