ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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DNA annealing helicase and endonuclease ZRANB3

Intramolecular
Cysteine 965 and cysteine 968
Cysteine 965 and cysteine 1044
Cysteine 965 and cysteine 1041
Cysteine 968 and cysteine 1041
Cysteine 968 and cysteine 1044
Cysteine 1041 and cysteine 1044
A redox-regulated disulphide may form within DNA annealing helicase and endonuclease ZRANB3 between cysteines 965 and 968 (20 and 23 respectively in this structure).

Details

Redox score ?
90
PDB code
5mkw
Structure name
crystal structure of the human zranb3 hnh domain
Structure deposition date
2016-12-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
3
% buried
34
Peptide accession
Q5FWF4
Residue number A
965
Residue number B
968
Peptide name
DNA annealing helicase and endonuclease ZRANB3

Ligandability

Cysteine 965 of DNA annealing helicase and endonuclease ZRANB3

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 968 of DNA annealing helicase and endonuclease ZRANB3

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 annealing helicase and endonuclease ZRANB3 between cysteines 965 and 1044 (20 and 99 respectively in this structure).

Details

Redox score ?
87
PDB code
5mkw
Structure name
crystal structure of the human zranb3 hnh domain
Structure deposition date
2016-12-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
3
% buried
36
Peptide accession
Q5FWF4
Residue number A
965
Residue number B
1044
Peptide name
DNA annealing helicase and endonuclease ZRANB3

Ligandability

Cysteine 965 of DNA annealing helicase and endonuclease ZRANB3

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 1044 of DNA annealing helicase and endonuclease ZRANB3

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 annealing helicase and endonuclease ZRANB3 between cysteines 965 and 1041 (20 and 96 respectively in this structure).

Details

Redox score ?
86
PDB code
5mkw
Structure name
crystal structure of the human zranb3 hnh domain
Structure deposition date
2016-12-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
3
% buried
48
Peptide accession
Q5FWF4
Residue number A
965
Residue number B
1041
Peptide name
DNA annealing helicase and endonuclease ZRANB3

Ligandability

Cysteine 965 of DNA annealing helicase and endonuclease ZRANB3

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 1041 of DNA annealing helicase and endonuclease ZRANB3

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 annealing helicase and endonuclease ZRANB3 between cysteines 968 and 1041 (23 and 96 respectively in this structure).

Details

Redox score ?
76
PDB code
5mkw
Structure name
crystal structure of the human zranb3 hnh domain
Structure deposition date
2016-12-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
37
Peptide accession
Q5FWF4
Residue number A
968
Residue number B
1041
Peptide name
DNA annealing helicase and endonuclease ZRANB3

Ligandability

Cysteine 968 of DNA annealing helicase and endonuclease ZRANB3

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 1041 of DNA annealing helicase and endonuclease ZRANB3

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 annealing helicase and endonuclease ZRANB3 between cysteines 968 and 1044 (23 and 99 respectively in this structure).

Details

Redox score ?
74
PDB code
5mkw
Structure name
crystal structure of the human zranb3 hnh domain
Structure deposition date
2016-12-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
24
Peptide accession
Q5FWF4
Residue number A
968
Residue number B
1044
Peptide name
DNA annealing helicase and endonuclease ZRANB3

Ligandability

Cysteine 968 of DNA annealing helicase and endonuclease ZRANB3

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 1044 of DNA annealing helicase and endonuclease ZRANB3

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 annealing helicase and endonuclease ZRANB3 between cysteines 1041 and 1044 (96 and 99 respectively in this structure).

Details

Redox score ?
69
PDB code
5mkw
Structure name
crystal structure of the human zranb3 hnh domain
Structure deposition date
2016-12-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
40
Peptide accession
Q5FWF4
Residue number A
1041
Residue number B
1044
Peptide name
DNA annealing helicase and endonuclease ZRANB3

Ligandability

Cysteine 1041 of DNA annealing helicase and endonuclease ZRANB3

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 1044 of DNA annealing helicase and endonuclease ZRANB3

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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