ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Transcription termination factor 4, mitochondrial

Intramolecular
Cysteine 182 and cysteine 183
Cysteine 182 and cysteine 219
Cysteine 183 and cysteine 219
A redox-regulated disulphide may form within Transcription termination factor 4, mitochondrial between cysteines 182 and 183. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
4fp9
Structure name
human mterf4-nsun4 protein complex
Structure deposition date
2012-06-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
36
Peptide accession
Q7Z6M4
Residue number A
182
Residue number B
183
Peptide name
Transcription termination factor 4, mitochondrial

Ligandability

Cysteine 182 of Transcription termination factor 4, mitochondrial

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 183 of Transcription termination factor 4, mitochondrial

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 Transcription termination factor 4, mitochondrial between cysteines 182 and 219. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4fzv
Structure name
crystal structure of the human mterf4:nsun4:sam ternary complex
Structure deposition date
2012-07-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
42
Peptide accession
Q7Z6M4
Residue number A
182
Residue number B
219
Peptide name
Transcription termination factor 4, mitochondrial

Ligandability

Cysteine 182 of Transcription termination factor 4, mitochondrial

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 219 of Transcription termination factor 4, mitochondrial

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 Transcription termination factor 4, mitochondrial between cysteines 183 and 219. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7of0
Structure name
structure of a human mitochondrial ribosome large subunit assembly intermediate in complex with mterf4-nsun4 (dataset1)
Structure deposition date
2021-05-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
11
% buried
57
Peptide accession
Q7Z6M4
Residue number A
183
Residue number B
219
Peptide name
Transcription termination factor 4, mitochondrial

Ligandability

Cysteine 183 of Transcription termination factor 4, mitochondrial

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 219 of Transcription termination factor 4, mitochondrial

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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