ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Transcription initiation factor TFIID subunit 1

Intramolecular
Cysteine 1364 and cysteine 1619 L
Cysteine 885 and cysteine 886
Cysteine 786 and cysteine 1066
A redox-regulated disulphide may form within Transcription initiation factor TFIID subunit 1 between cysteines 1364 and 1619.

Details

Redox score ?
84
PDB code
3aad
Structure name
structure of the histone chaperone cia/asf1-double bromodomain complex linking histone modifications and site-specific histone eviction
Structure deposition date
2009-11-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P21675
Residue number A
1364
Residue number B
1619
Peptide name
Transcription initiation factor TFIID subunit 1

Ligandability

Cysteine 1364 of Transcription initiation factor TFIID subunit 1

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.

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 1619 of Transcription initiation factor TFIID subunit 1

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 initiation factor TFIID subunit 1 between cysteines 885 and 886 (906 and 907 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
4rgw
Structure name
crystal structure of a taf1-taf7 complex in human transcription factor iid
Structure deposition date
2014-09-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
13
% buried
100
Peptide accession
P21675
Residue number A
885
Residue number B
886
Peptide name
Transcription initiation factor TFIID subunit 1

Ligandability

Cysteine 885 of Transcription initiation factor TFIID subunit 1

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 886 of Transcription initiation factor TFIID subunit 1

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 initiation factor TFIID subunit 1 between cysteines 786 and 1066. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
6mzl
Structure name
human tfiid canonical state
Structure deposition date
2018-11-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
86
Peptide accession
P21675
Residue number A
786
Residue number B
1066
Peptide name
Transcription initiation factor TFIID subunit 1

Ligandability

Cysteine 786 of Transcription initiation factor TFIID subunit 1

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 1066 of Transcription initiation factor TFIID subunit 1

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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