ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

RNA polymerase-associated protein CTR9 homolog

Intermolecular
Cysteine 511 and cysteine 266 of SKI8 subunit of superkiller complex protein
Intramolecular
Cysteine 136 and cysteine 138 L
Cysteine 136 and cysteine 171 L
A redox-regulated disulphide may form between cysteine 511 of RNA polymerase-associated protein CTR9 homolog and cysteine 266 of SKI8 subunit of superkiller complex protein. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6ted
Structure name
structure of complete, activated transcription complex pol ii-dsif- paf-spt6 uncovers allosteric elongation activation by rtf1
Structure deposition date
2019-11-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
60
Peptide A name
RNA polymerase-associated protein CTR9 homolog
Peptide B name
SKI8 subunit of superkiller complex protein
Peptide A accession
Q6PD62
Peptide B accession
Q9GZS3
Peptide A residue number
511
Peptide B residue number
266

Ligandability

Cysteine 511 of RNA polymerase-associated protein CTR9 homolog

Cysteine 266 of SKI8 subunit of superkiller complex protein

A redox-regulated disulphide may form within RNA polymerase-associated protein CTR9 homolog between cysteines 136 and 138. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6ted
Structure name
structure of complete, activated transcription complex pol ii-dsif- paf-spt6 uncovers allosteric elongation activation by rtf1
Structure deposition date
2019-11-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
58
Peptide accession
Q6PD62
Residue number A
136
Residue number B
138
Peptide name
RNA polymerase-associated protein CTR9 homolog

Ligandability

Cysteine 136 of RNA polymerase-associated protein CTR9 homolog

Cysteine 138 of RNA polymerase-associated protein CTR9 homolog

A redox-regulated disulphide may form within RNA polymerase-associated protein CTR9 homolog between cysteines 136 and 171. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
6ted
Structure name
structure of complete, activated transcription complex pol ii-dsif- paf-spt6 uncovers allosteric elongation activation by rtf1
Structure deposition date
2019-11-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
Q6PD62
Residue number A
136
Residue number B
171
Peptide name
RNA polymerase-associated protein CTR9 homolog

Ligandability

Cysteine 136 of RNA polymerase-associated protein CTR9 homolog

Cysteine 171 of RNA polymerase-associated protein CTR9 homolog

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