ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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DNA repair protein REV1

Intramolecular
Cysteine 958 and cysteine 977
Cysteine 668 and cysteine 695
Cysteine 426 and cysteine 511
Cysteine 426 and cysteine 604
Cysteine 511 and cysteine 533
A redox-regulated disulphide may form within DNA repair protein REV1 between cysteines 958 and 977 (957 and 976 respectively in this structure).

Details

Redox score ?
88
PDB code
5vzm
Structure name
solution nmr structure of human rev1 (932-1039) in complex with ubiquitin
Structure deposition date
2017-05-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UBZ9
Residue number A
958
Residue number B
977
Peptide name
DNA repair protein REV1

Ligandability

Cysteine 958 of DNA repair protein REV1

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 977 of DNA repair protein REV1

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 repair protein REV1 between cysteines 668 and 695. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
3gqc
Structure name
structure of human rev1-dna-dntp ternary complex
Structure deposition date
2009-03-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
67
Peptide accession
Q9UBZ9
Residue number A
668
Residue number B
695
Peptide name
DNA repair protein REV1

Ligandability

Cysteine 668 of DNA repair protein REV1

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 695 of DNA repair protein REV1

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 repair protein REV1 between cysteines 426 and 511. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3gqc
Structure name
structure of human rev1-dna-dntp ternary complex
Structure deposition date
2009-03-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
90
Peptide accession
Q9UBZ9
Residue number A
426
Residue number B
511
Peptide name
DNA repair protein REV1

Ligandability

Cysteine 426 of DNA repair protein REV1

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 511 of DNA repair protein REV1

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 repair protein REV1 between cysteines 426 and 604. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3gqc
Structure name
structure of human rev1-dna-dntp ternary complex
Structure deposition date
2009-03-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
88
Peptide accession
Q9UBZ9
Residue number A
426
Residue number B
604
Peptide name
DNA repair protein REV1

Ligandability

Cysteine 426 of DNA repair protein REV1

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 604 of DNA repair protein REV1

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 repair protein REV1 between cysteines 511 and 533. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3gqc
Structure name
structure of human rev1-dna-dntp ternary complex
Structure deposition date
2009-03-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
64
Peptide accession
Q9UBZ9
Residue number A
511
Residue number B
533
Peptide name
DNA repair protein REV1

Ligandability

Cysteine 511 of DNA repair protein REV1

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 533 of DNA repair protein REV1

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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