ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

Intramolecular
Cysteine 341 and cysteine 350
Cysteine 352 and cysteine 411
Cysteine 341 and cysteine 522 L
Cysteine 350 and cysteine 522 L
A redox-regulated disulphide may form within Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 between cysteines 341 and 350.

Details

Redox score ?
77
PDB code
4qfx
Structure name
crystal structure of the tetrameric dgtp/datp-bound samhd1 (rn206) mutant catalytic core
Structure deposition date
2014-05-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
75
Minimum pKa ?
7
% buried
74
Peptide accession
Q9Y3Z3
Residue number A
341
Residue number B
350
Peptide name
Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

Ligandability

Cysteine 341 of Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

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 350 of Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

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 Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 between cysteines 352 and 411. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
6brg
Structure name
the sam domain of mouse samhd1 is critical for its activation and regulation
Structure deposition date
2017-11-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
86
Peptide accession
F8WJE0
Residue number A
352
Residue number B
411
Peptide name
Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

Ligandability

Cysteine 352 of Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

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 411 of Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

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 Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 between cysteines 341 and 522. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4qg0
Structure name
crystal structure of the tetrameric dgtp/dutp-bound samhd1 (rn206) mutant catalytic core
Structure deposition date
2014-05-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
8
% buried
58
Peptide accession
Q9Y3Z3
Residue number A
341
Residue number B
522
Peptide name
Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

Ligandability

Cysteine 341 of Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

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 522 of Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

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 Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 between cysteines 350 and 522. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4qg2
Structure name
crystal structure of the tetrameric gtp/datp/atp-bound samhd1 (rn206) mutant catalytic core
Structure deposition date
2014-05-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
12
% buried
nan
Peptide accession
Q9Y3Z3
Residue number A
350
Residue number B
522
Peptide name
Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

Ligandability

Cysteine 350 of Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

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 522 of Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

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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