ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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ATP-dependent DNA helicase Q1

Intramolecular
Cysteine 453 and cysteine 478
Cysteine 471 and cysteine 475 L
Cysteine 453 and cysteine 471
Cysteine 453 and cysteine 475 L
Cysteine 475 and cysteine 478 L
Cysteine 471 and cysteine 478
Cysteine 475 and cysteine 479 L
Cysteine 471 and cysteine 479
Cysteine 478 and cysteine 479
Cysteine 453 and cysteine 479
More...
Cysteine 223 and cysteine 224
Cysteine 224 and cysteine 270
Cysteine 138 and cysteine 223
A redox-regulated disulphide may form within ATP-dependent DNA helicase Q1 between cysteines 453 and 478.

Details

Redox score ?
86
PDB code
4u7d
Structure name
structure of human recq-like helicase in complex with an oligonucleotide
Structure deposition date
2014-07-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
58
Minimum pKa ?
6
% buried
34
Peptide accession
P46063
Residue number A
453
Residue number B
478
Peptide name
ATP-dependent DNA helicase Q1

Ligandability

Cysteine 453 of ATP-dependent DNA helicase Q1

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 478 of ATP-dependent DNA helicase Q1

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 Q1 between cysteines 471 and 475.

Details

Redox score ?
84
PDB code
2wwy
Structure name
structure of human recq-like helicase in complex with a dna substrate
Structure deposition date
2009-10-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
34
Peptide accession
P46063
Residue number A
471
Residue number B
475
Peptide name
ATP-dependent DNA helicase Q1

Ligandability

Cysteine 471 of ATP-dependent DNA helicase Q1

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 475 of ATP-dependent DNA helicase Q1

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 Q1 between cysteines 453 and 471.

Details

Redox score ?
81
PDB code
4u7d
Structure name
structure of human recq-like helicase in complex with an oligonucleotide
Structure deposition date
2014-07-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
8
% buried
40
Peptide accession
P46063
Residue number A
453
Residue number B
471
Peptide name
ATP-dependent DNA helicase Q1

Ligandability

Cysteine 453 of ATP-dependent DNA helicase Q1

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 471 of ATP-dependent DNA helicase Q1

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 Q1 between cysteines 453 and 475.

Details

Redox score ?
81
PDB code
6jtz
Structure name
crystal structure of hrecq1_d2-zn-wh containing mutation on beta- hairpin
Structure deposition date
2019-04-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
6
% buried
36
Peptide accession
P46063
Residue number A
453
Residue number B
475
Peptide name
ATP-dependent DNA helicase Q1

Ligandability

Cysteine 453 of ATP-dependent DNA helicase Q1

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 475 of ATP-dependent DNA helicase Q1

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 Q1 between cysteines 475 and 478.

Details

Redox score ?
79
PDB code
4u7d
Structure name
structure of human recq-like helicase in complex with an oligonucleotide
Structure deposition date
2014-07-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
40
Peptide accession
P46063
Residue number A
475
Residue number B
478
Peptide name
ATP-dependent DNA helicase Q1

Ligandability

Cysteine 475 of ATP-dependent DNA helicase Q1

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 478 of ATP-dependent DNA helicase Q1

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 Q1 between cysteines 471 and 478.

Details

Redox score ?
78
PDB code
4u7d
Structure name
structure of human recq-like helicase in complex with an oligonucleotide
Structure deposition date
2014-07-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
10
% buried
27
Peptide accession
P46063
Residue number A
471
Residue number B
478
Peptide name
ATP-dependent DNA helicase Q1

Ligandability

Cysteine 471 of ATP-dependent DNA helicase Q1

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 478 of ATP-dependent DNA helicase Q1

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 Q1 between cysteines 475 and 479.

Details

Redox score ?
70
PDB code
6jtz
Structure name
crystal structure of hrecq1_d2-zn-wh containing mutation on beta- hairpin
Structure deposition date
2019-04-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
53
Minimum pKa ?
6
% buried
22
Peptide accession
P46063
Residue number A
475
Residue number B
479
Peptide name
ATP-dependent DNA helicase Q1

Ligandability

Cysteine 475 of ATP-dependent DNA helicase Q1

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 479 of ATP-dependent DNA helicase Q1

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 Q1 between cysteines 471 and 479.

Details

Redox score ?
67
PDB code
2v1x
Structure name
crystal structure of human recq-like dna helicase
Structure deposition date
2007-05-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
45
Minimum pKa ?
6
% buried
18
Peptide accession
P46063
Residue number A
471
Residue number B
479
Peptide name
ATP-dependent DNA helicase Q1

Ligandability

Cysteine 471 of ATP-dependent DNA helicase Q1

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 479 of ATP-dependent DNA helicase Q1

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 Q1 between cysteines 478 and 479. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
4u7d
Structure name
structure of human recq-like helicase in complex with an oligonucleotide
Structure deposition date
2014-07-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
8
Peptide accession
P46063
Residue number A
478
Residue number B
479
Peptide name
ATP-dependent DNA helicase Q1

Ligandability

Cysteine 478 of ATP-dependent DNA helicase Q1

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 479 of ATP-dependent DNA helicase Q1

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 Q1 between cysteines 453 and 479. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2wwy
Structure name
structure of human recq-like helicase in complex with a dna substrate
Structure deposition date
2009-10-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
16
Peptide accession
P46063
Residue number A
453
Residue number B
479
Peptide name
ATP-dependent DNA helicase Q1

Ligandability

Cysteine 453 of ATP-dependent DNA helicase Q1

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 479 of ATP-dependent DNA helicase Q1

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 Q1 between cysteines 223 and 224. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2v1x
Structure name
crystal structure of human recq-like dna helicase
Structure deposition date
2007-05-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
72
Peptide accession
P46063
Residue number A
223
Residue number B
224
Peptide name
ATP-dependent DNA helicase Q1

Ligandability

Cysteine 223 of ATP-dependent DNA helicase Q1

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 224 of ATP-dependent DNA helicase Q1

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 Q1 between cysteines 224 and 270. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
2v1x
Structure name
crystal structure of human recq-like dna helicase
Structure deposition date
2007-05-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
47
Peptide accession
P46063
Residue number A
224
Residue number B
270
Peptide name
ATP-dependent DNA helicase Q1

Ligandability

Cysteine 224 of ATP-dependent DNA helicase Q1

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 270 of ATP-dependent DNA helicase Q1

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 Q1 between cysteines 138 and 223. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
2v1x
Structure name
crystal structure of human recq-like dna helicase
Structure deposition date
2007-05-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
78
Peptide accession
P46063
Residue number A
138
Residue number B
223
Peptide name
ATP-dependent DNA helicase Q1

Ligandability

Cysteine 138 of ATP-dependent DNA helicase Q1

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 223 of ATP-dependent DNA helicase Q1

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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