ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Bifunctional polynucleotide phosphatase/kinase

Intramolecular
Cysteine 408 and cysteine 436 L
Cysteine 404 and cysteine 408 L
Cysteine 404 and cysteine 436 L
Cysteine 436 and cysteine 444
Cysteine 444 and cysteine 446
Cysteine 408 and cysteine 444 L
A redox-regulated disulphide may form within Bifunctional polynucleotide phosphatase/kinase between cysteines 408 and 436.

Details

Redox score ?
76
PDB code
3u7h
Structure name
crystal structure of mpnkp catalytic fragment (d170a) bound to single- stranded dna (tccttp)
Structure deposition date
2011-10-13
Thiol separation (Å)
3
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
50
Peptide accession
Q9JLV6
Residue number A
408
Residue number B
436
Peptide name
Bifunctional polynucleotide phosphatase/kinase

Ligandability

Cysteine 408 of Bifunctional polynucleotide phosphatase/kinase

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 436 of Bifunctional polynucleotide phosphatase/kinase

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 Bifunctional polynucleotide phosphatase/kinase between cysteines 404 and 408. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
3u7h
Structure name
crystal structure of mpnkp catalytic fragment (d170a) bound to single- stranded dna (tccttp)
Structure deposition date
2011-10-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
40
Peptide accession
Q9JLV6
Residue number A
404
Residue number B
408
Peptide name
Bifunctional polynucleotide phosphatase/kinase

Ligandability

Cysteine 404 of Bifunctional polynucleotide phosphatase/kinase

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 408 of Bifunctional polynucleotide phosphatase/kinase

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 Bifunctional polynucleotide phosphatase/kinase between cysteines 404 and 436. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
3u7f
Structure name
crystal structure of mpnkp catalytic fragment (d170a) bound to single- stranded dna (tcctcp)
Structure deposition date
2011-10-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
7
% buried
41
Peptide accession
Q9JLV6
Residue number A
404
Residue number B
436
Peptide name
Bifunctional polynucleotide phosphatase/kinase

Ligandability

Cysteine 404 of Bifunctional polynucleotide phosphatase/kinase

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 436 of Bifunctional polynucleotide phosphatase/kinase

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 Bifunctional polynucleotide phosphatase/kinase between cysteines 436 and 444. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
3u7g
Structure name
crystal structure of mpnkp catalytic fragment (d170a) bound to single- stranded dna (tcctap)
Structure deposition date
2011-10-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
7
% buried
63
Peptide accession
Q9JLV6
Residue number A
436
Residue number B
444
Peptide name
Bifunctional polynucleotide phosphatase/kinase

Ligandability

Cysteine 436 of Bifunctional polynucleotide phosphatase/kinase

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 444 of Bifunctional polynucleotide phosphatase/kinase

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 Bifunctional polynucleotide phosphatase/kinase between cysteines 444 and 446. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3u7h
Structure name
crystal structure of mpnkp catalytic fragment (d170a) bound to single- stranded dna (tccttp)
Structure deposition date
2011-10-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
86
Minimum pKa ?
13
% buried
91
Peptide accession
Q9JLV6
Residue number A
444
Residue number B
446
Peptide name
Bifunctional polynucleotide phosphatase/kinase

Ligandability

Cysteine 444 of Bifunctional polynucleotide phosphatase/kinase

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 446 of Bifunctional polynucleotide phosphatase/kinase

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 Bifunctional polynucleotide phosphatase/kinase between cysteines 408 and 444. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3u7e
Structure name
crystal structure of mpnkp catalytic fragment (d170a)
Structure deposition date
2011-10-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
82
Minimum pKa ?
13
% buried
77
Peptide accession
Q9JLV6
Residue number A
408
Residue number B
444
Peptide name
Bifunctional polynucleotide phosphatase/kinase

Ligandability

Cysteine 408 of Bifunctional polynucleotide phosphatase/kinase

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 444 of Bifunctional polynucleotide phosphatase/kinase

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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