ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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ATP-dependent DNA helicase Q4

Intramolecular
Cysteine 853 and cysteine 897 L
Cysteine 855 and cysteine 897 L
Cysteine 853 and cysteine 855 L
Cysteine 1085 and cysteine 1088
Cysteine 853 and cysteine 857 L
Cysteine 855 and cysteine 857 L
Cysteine 963 and cysteine 969
Cysteine 945 and cysteine 963
Cysteine 963 and cysteine 1008
Cysteine 945 and cysteine 969
More...
Cysteine 945 and cysteine 1008
Cysteine 620 and cysteine 925
Cysteine 609 and cysteine 620
Cysteine 511 and cysteine 603 L
A redox-regulated disulphide may form within ATP-dependent DNA helicase Q4 between cysteines 853 and 897.

Details

Redox score ?
87
PDB code
5lst
Structure name
crystal structure of the human recql4 helicase
Structure deposition date
2016-09-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
7
% buried
18
Peptide accession
O94761
Residue number A
853
Residue number B
897
Peptide name
ATP-dependent DNA helicase Q4

Ligandability

Cysteine 853 of ATP-dependent DNA helicase Q4

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 897 of ATP-dependent DNA helicase Q4

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 ATP-dependent DNA helicase Q4 between cysteines 855 and 897.

Details

Redox score ?
83
PDB code
5lst
Structure name
crystal structure of the human recql4 helicase
Structure deposition date
2016-09-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
7
% buried
14
Peptide accession
O94761
Residue number A
855
Residue number B
897
Peptide name
ATP-dependent DNA helicase Q4

Ligandability

Cysteine 855 of ATP-dependent DNA helicase Q4

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 897 of ATP-dependent DNA helicase Q4

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 ATP-dependent DNA helicase Q4 between cysteines 853 and 855.

Details

Redox score ?
80
PDB code
5lst
Structure name
crystal structure of the human recql4 helicase
Structure deposition date
2016-09-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
12
Peptide accession
O94761
Residue number A
853
Residue number B
855
Peptide name
ATP-dependent DNA helicase Q4

Ligandability

Cysteine 853 of ATP-dependent DNA helicase Q4

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 855 of ATP-dependent DNA helicase Q4

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within ATP-dependent DNA helicase Q4 between cysteines 1085 and 1088.

Details

Redox score ?
60
PDB code
5lst
Structure name
crystal structure of the human recql4 helicase
Structure deposition date
2016-09-05
Thiol separation (Å)
6
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
59
Peptide accession
O94761
Residue number A
1085
Residue number B
1088
Peptide name
ATP-dependent DNA helicase Q4

Ligandability

Cysteine 1085 of ATP-dependent DNA helicase Q4

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 1088 of ATP-dependent DNA helicase Q4

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 ATP-dependent DNA helicase Q4 between cysteines 853 and 857. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
5lst
Structure name
crystal structure of the human recql4 helicase
Structure deposition date
2016-09-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
8
Peptide accession
O94761
Residue number A
853
Residue number B
857
Peptide name
ATP-dependent DNA helicase Q4

Ligandability

Cysteine 853 of ATP-dependent DNA helicase Q4

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 857 of ATP-dependent DNA helicase Q4

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within ATP-dependent DNA helicase Q4 between cysteines 855 and 857. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
5lst
Structure name
crystal structure of the human recql4 helicase
Structure deposition date
2016-09-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
4
Peptide accession
O94761
Residue number A
855
Residue number B
857
Peptide name
ATP-dependent DNA helicase Q4

Ligandability

Cysteine 855 of ATP-dependent DNA helicase Q4

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 857 of ATP-dependent DNA helicase Q4

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within ATP-dependent DNA helicase Q4 between cysteines 963 and 969. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
5lst
Structure name
crystal structure of the human recql4 helicase
Structure deposition date
2016-09-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
11
% buried
58
Peptide accession
O94761
Residue number A
963
Residue number B
969
Peptide name
ATP-dependent DNA helicase Q4

Ligandability

Cysteine 963 of ATP-dependent DNA helicase Q4

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 969 of ATP-dependent DNA helicase Q4

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 ATP-dependent DNA helicase Q4 between cysteines 945 and 963. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
5lst
Structure name
crystal structure of the human recql4 helicase
Structure deposition date
2016-09-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
11
% buried
64
Peptide accession
O94761
Residue number A
945
Residue number B
963
Peptide name
ATP-dependent DNA helicase Q4

Ligandability

Cysteine 945 of ATP-dependent DNA helicase Q4

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 963 of ATP-dependent DNA helicase Q4

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 ATP-dependent DNA helicase Q4 between cysteines 963 and 1008. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
5lst
Structure name
crystal structure of the human recql4 helicase
Structure deposition date
2016-09-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
41
Peptide accession
O94761
Residue number A
963
Residue number B
1008
Peptide name
ATP-dependent DNA helicase Q4

Ligandability

Cysteine 963 of ATP-dependent DNA helicase Q4

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 1008 of ATP-dependent DNA helicase Q4

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 ATP-dependent DNA helicase Q4 between cysteines 945 and 969. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
5lst
Structure name
crystal structure of the human recql4 helicase
Structure deposition date
2016-09-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
62
Peptide accession
O94761
Residue number A
945
Residue number B
969
Peptide name
ATP-dependent DNA helicase Q4

Ligandability

Cysteine 945 of ATP-dependent DNA helicase Q4

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 969 of ATP-dependent DNA helicase Q4

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 ATP-dependent DNA helicase Q4 between cysteines 945 and 1008. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
5lst
Structure name
crystal structure of the human recql4 helicase
Structure deposition date
2016-09-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
44
Peptide accession
O94761
Residue number A
945
Residue number B
1008
Peptide name
ATP-dependent DNA helicase Q4

Ligandability

Cysteine 945 of ATP-dependent DNA helicase Q4

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 1008 of ATP-dependent DNA helicase Q4

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 ATP-dependent DNA helicase Q4 between cysteines 620 and 925. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5lst
Structure name
crystal structure of the human recql4 helicase
Structure deposition date
2016-09-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
84
Peptide accession
O94761
Residue number A
620
Residue number B
925
Peptide name
ATP-dependent DNA helicase Q4

Ligandability

Cysteine 620 of ATP-dependent DNA helicase Q4

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 925 of ATP-dependent DNA helicase Q4

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 ATP-dependent DNA helicase Q4 between cysteines 609 and 620. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5lst
Structure name
crystal structure of the human recql4 helicase
Structure deposition date
2016-09-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
81
Peptide accession
O94761
Residue number A
609
Residue number B
620
Peptide name
ATP-dependent DNA helicase Q4

Ligandability

Cysteine 609 of ATP-dependent DNA helicase Q4

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 620 of ATP-dependent DNA helicase Q4

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 ATP-dependent DNA helicase Q4 between cysteines 511 and 603. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
5lst
Structure name
crystal structure of the human recql4 helicase
Structure deposition date
2016-09-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
93
Minimum pKa ?
12
% buried
92
Peptide accession
O94761
Residue number A
511
Residue number B
603
Peptide name
ATP-dependent DNA helicase Q4

Ligandability

Cysteine 511 of ATP-dependent DNA helicase Q4

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 603 of ATP-dependent DNA helicase Q4

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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