ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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ATP-dependent DNA helicase PIF1

Intramolecular
Cysteine 399 and cysteine 603
Cysteine 360 and cysteine 369
Cysteine 261 and cysteine 467
A redox-regulated disulphide may form within ATP-dependent DNA helicase PIF1 between cysteines 399 and 603. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
6hph
Structure name
crystal structure of human pif1 helicase in complex with amp-pnp
Structure deposition date
2018-09-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
48
Peptide accession
Q9H611
Residue number A
399
Residue number B
603
Peptide name
ATP-dependent DNA helicase PIF1

Ligandability

Cysteine 399 of ATP-dependent DNA helicase PIF1

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 603 of ATP-dependent DNA helicase PIF1

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 PIF1 between cysteines 360 and 369. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6hpq
Structure name
crystal structure of human pif1 helicase in complex with amp-pnp, brominated crystal form
Structure deposition date
2018-09-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
83
Peptide accession
Q9H611
Residue number A
360
Residue number B
369
Peptide name
ATP-dependent DNA helicase PIF1

Ligandability

Cysteine 360 of ATP-dependent DNA helicase PIF1

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 369 of ATP-dependent DNA helicase PIF1

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 PIF1 between cysteines 261 and 467. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
5fhh
Structure name
structure of human pif1 helicase domain residues 200-641
Structure deposition date
2015-12-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
62
Peptide accession
Q9H611
Residue number A
261
Residue number B
467
Peptide name
ATP-dependent DNA helicase PIF1

Ligandability

Cysteine 261 of ATP-dependent DNA helicase PIF1

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 467 of ATP-dependent DNA helicase PIF1

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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