ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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DNA-directed RNA polymerase I subunit RPA43

Intramolecular
Cysteine 38 and cysteine 150
Cysteine 47 and cysteine 124
Cysteine 28 and cysteine 150
A redox-regulated disulphide may form within DNA-directed RNA polymerase I subunit RPA43 between cysteines 38 and 150. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
7ob9
Structure name
cryo-em structure of human rna polymerase i in elongation state
Structure deposition date
2021-04-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
37
Peptide accession
Q3B726
Residue number A
38
Residue number B
150
Peptide name
DNA-directed RNA polymerase I subunit RPA43

Ligandability

Cysteine 38 of DNA-directed RNA polymerase I subunit RPA43

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 150 of DNA-directed RNA polymerase I subunit RPA43

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-directed RNA polymerase I subunit RPA43 between cysteines 47 and 124. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
7oba
Structure name
cryo-em structure of human rna polymerase i in complex with rrn3
Structure deposition date
2021-04-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
33
Peptide accession
Q3B726
Residue number A
47
Residue number B
124
Peptide name
DNA-directed RNA polymerase I subunit RPA43

Ligandability

Cysteine 47 of DNA-directed RNA polymerase I subunit RPA43

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 124 of DNA-directed RNA polymerase I subunit RPA43

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-directed RNA polymerase I subunit RPA43 between cysteines 28 and 150. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
7ob9
Structure name
cryo-em structure of human rna polymerase i in elongation state
Structure deposition date
2021-04-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
11
% buried
nan
Peptide accession
Q3B726
Residue number A
28
Residue number B
150
Peptide name
DNA-directed RNA polymerase I subunit RPA43

Ligandability

Cysteine 28 of DNA-directed RNA polymerase I subunit RPA43

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 150 of DNA-directed RNA polymerase I subunit RPA43

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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