ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

DNA repair protein complementing XP-A cells

Intramolecular
Cysteine 105 and cysteine 108
Cysteine 105 and cysteine 129
Cysteine 105 and cysteine 126
Cysteine 108 and cysteine 126
Cysteine 126 and cysteine 129
Cysteine 108 and cysteine 129
A redox-regulated disulphide may form within DNA repair protein complementing XP-A cells between cysteines 105 and 108.

Details

Redox score ?
89
PDB code
6j44
Structure name
crystal structure of the redefined dna-binding domain of human xpa
Structure deposition date
2019-01-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
5
% buried
0
Peptide accession
P23025
Residue number A
105
Residue number B
108
Peptide name
DNA repair protein complementing XP-A cells

Ligandability

Cysteine 105 of DNA repair protein complementing XP-A cells

Cysteine 108 of DNA repair protein complementing XP-A cells

A redox-regulated disulphide may form within DNA repair protein complementing XP-A cells between cysteines 105 and 129.

Details

Redox score ?
87
PDB code
6j44
Structure name
crystal structure of the redefined dna-binding domain of human xpa
Structure deposition date
2019-01-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
5
% buried
0
Peptide accession
P23025
Residue number A
105
Residue number B
129
Peptide name
DNA repair protein complementing XP-A cells

Ligandability

Cysteine 105 of DNA repair protein complementing XP-A cells

Cysteine 129 of DNA repair protein complementing XP-A cells

A redox-regulated disulphide may form within DNA repair protein complementing XP-A cells between cysteines 105 and 126.

Details

Redox score ?
86
PDB code
6j44
Structure name
crystal structure of the redefined dna-binding domain of human xpa
Structure deposition date
2019-01-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
5
% buried
0
Peptide accession
P23025
Residue number A
105
Residue number B
126
Peptide name
DNA repair protein complementing XP-A cells

Ligandability

Cysteine 105 of DNA repair protein complementing XP-A cells

Cysteine 126 of DNA repair protein complementing XP-A cells

A redox-regulated disulphide may form within DNA repair protein complementing XP-A cells between cysteines 108 and 126.

Details

Redox score ?
84
PDB code
6lae
Structure name
crystal structure of the dna-binding domain of human xpa in complex with dna
Structure deposition date
2019-11-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
45
Minimum pKa ?
7
% buried
0
Peptide accession
P23025
Residue number A
108
Residue number B
126
Peptide name
DNA repair protein complementing XP-A cells

Ligandability

Cysteine 108 of DNA repair protein complementing XP-A cells

Cysteine 126 of DNA repair protein complementing XP-A cells

A redox-regulated disulphide may form within DNA repair protein complementing XP-A cells between cysteines 126 and 129.

Details

Redox score ?
84
PDB code
6lae
Structure name
crystal structure of the dna-binding domain of human xpa in complex with dna
Structure deposition date
2019-11-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
54
Minimum pKa ?
7
% buried
0
Peptide accession
P23025
Residue number A
126
Residue number B
129
Peptide name
DNA repair protein complementing XP-A cells

Ligandability

Cysteine 126 of DNA repair protein complementing XP-A cells

Cysteine 129 of DNA repair protein complementing XP-A cells

A redox-regulated disulphide may form within DNA repair protein complementing XP-A cells between cysteines 108 and 129.

Details

Redox score ?
82
PDB code
6lae
Structure name
crystal structure of the dna-binding domain of human xpa in complex with dna
Structure deposition date
2019-11-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
40
Minimum pKa ?
9
% buried
0
Peptide accession
P23025
Residue number A
108
Residue number B
129
Peptide name
DNA repair protein complementing XP-A cells

Ligandability

Cysteine 108 of DNA repair protein complementing XP-A cells

Cysteine 129 of DNA repair protein complementing XP-A cells

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