ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Protein artemis

Intramolecular
Cysteine 256 and cysteine 272
Cysteine 182 and cysteine 315
Cysteine 333 and cysteine 359
Cysteine 34 and cysteine 61
Cysteine 34 and cysteine 116
Cysteine 206 and cysteine 256
Cysteine 182 and cysteine 206
A redox-regulated disulphide may form within Protein artemis between cysteines 256 and 272.

Details

Redox score ?
90
PDB code
7apv
Structure name
structure of artemis/dclre1c/snm1c in complex with ceftriaxone
Structure deposition date
2020-10-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
1
% buried
58
Peptide accession
Q96SD1
Residue number A
256
Residue number B
272
Peptide name
Protein artemis

Ligandability

Cysteine 256 of Protein artemis

Cysteine 272 of Protein artemis

A redox-regulated disulphide may form within Protein artemis between cysteines 182 and 315.

Details

Redox score ?
76
PDB code
7af1
Structure name
the structure of artemis/snm1c/dclre1c with 2 zinc ions
Structure deposition date
2020-09-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
7
% buried
72
Peptide accession
Q96SD1
Residue number A
182
Residue number B
315
Peptide name
Protein artemis

Ligandability

Cysteine 182 of Protein artemis

Cysteine 315 of Protein artemis

A redox-regulated disulphide may form within Protein artemis between cysteines 333 and 359. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
6wo0
Structure name
human artemis/snm1c catalytic domain, crystal form 1
Structure deposition date
2020-04-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
22
Peptide accession
Q96SD1
Residue number A
333
Residue number B
359
Peptide name
Protein artemis

Ligandability

Cysteine 333 of Protein artemis

Cysteine 359 of Protein artemis

A redox-regulated disulphide may form within Protein artemis between cysteines 34 and 61. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6wnl
Structure name
human artemis/snm1c catalytic domain, crystal form 2
Structure deposition date
2020-04-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
95
Peptide accession
Q96SD1
Residue number A
34
Residue number B
61
Peptide name
Protein artemis

Ligandability

Cysteine 34 of Protein artemis

Cysteine 61 of Protein artemis

A redox-regulated disulphide may form within Protein artemis between cysteines 34 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
7agi
Structure name
the structure of artemis variant h35d
Structure deposition date
2020-09-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
92
Peptide accession
Q96SD1
Residue number A
34
Residue number B
116
Peptide name
Protein artemis

Ligandability

Cysteine 34 of Protein artemis

Cysteine 116 of Protein artemis

A redox-regulated disulphide may form within Protein artemis between cysteines 206 and 256. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
7af1
Structure name
the structure of artemis/snm1c/dclre1c with 2 zinc ions
Structure deposition date
2020-09-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
13
% buried
86
Peptide accession
Q96SD1
Residue number A
206
Residue number B
256
Peptide name
Protein artemis

Ligandability

Cysteine 206 of Protein artemis

Cysteine 256 of Protein artemis

A redox-regulated disulphide may form within Protein artemis between cysteines 182 and 206. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
7sgl
Structure name
dna-pk complex of dna end processing
Structure deposition date
2021-10-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
13
% buried
100
Peptide accession
Q96SD1
Residue number A
182
Residue number B
206
Peptide name
Protein artemis

Ligandability

Cysteine 182 of Protein artemis

Cysteine 206 of Protein artemis

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