ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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General transcription factor II-I

Intramolecular
Cysteine 121 and cysteine 123
A redox-regulated disulphide may form within General transcription factor II-I between cysteines 121 and 123 (27 and 29 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2d9b
Structure name
solution structure of rsgi ruh-052, a gtf2i domain in human cdna
Structure deposition date
2005-12-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
36
Peptide accession
P78347
Residue number A
121
Residue number B
123
Peptide name
General transcription factor II-I

Ligandability

Cysteine 121 of General transcription factor II-I

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 123 of General transcription factor II-I

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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