Transcription initiation factor TFIID subunit 3
Intramolecular
Cysteine 885 and cysteine 888
Cysteine 885 and cysteine 914
Cysteine 885 and cysteine 911
Cysteine 868 and cysteine 871
Cysteine 888 and cysteine 911
Cysteine 911 and cysteine 914
Cysteine 868 and cysteine 894
Cysteine 888 and cysteine 914
Cysteine 871 and cysteine 894
Cysteine 870 and cysteine 911
More...Cysteine 870 and cysteine 885
Cysteine 870 and cysteine 888
Cysteine 18 and cysteine 31
2k16 A 885 A 888
A redox-regulated disulphide may form within Transcription initiation factor TFIID subunit 3 between cysteines 885 and 888.
Details
Redox score ?
88
PDB code
2k16
Structure name
solution structure of the free taf3 phd domain
Structure deposition date
2008-02-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
6
% buried
10
Peptide accession
Q5HZG4
Residue number A
885
Residue number B
888
Peptide name
Transcription initiation factor TFIID subunit 3
Ligandability
Cysteine 885 of Transcription initiation factor TFIID subunit 3
Cysteine 888 of Transcription initiation factor TFIID subunit 3
2k16 A 885 A 914
A redox-regulated disulphide may form within Transcription initiation factor TFIID subunit 3 between cysteines 885 and 914.
Details
Redox score ?
87
PDB code
2k16
Structure name
solution structure of the free taf3 phd domain
Structure deposition date
2008-02-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
6
Peptide accession
Q5HZG4
Residue number A
885
Residue number B
914
Peptide name
Transcription initiation factor TFIID subunit 3
Ligandability
Cysteine 885 of Transcription initiation factor TFIID subunit 3
Cysteine 914 of Transcription initiation factor TFIID subunit 3
2k17 A 885 A 911
A redox-regulated disulphide may form within Transcription initiation factor TFIID subunit 3 between cysteines 885 and 911.
Details
Redox score ?
85
PDB code
2k17
Structure name
solution structure of the taf3 phd domain in complex with a h3k4me3 peptide
Structure deposition date
2008-02-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
6
% buried
26
Peptide accession
Q5HZG4
Residue number A
885
Residue number B
911
Peptide name
Transcription initiation factor TFIID subunit 3
Ligandability
Cysteine 885 of Transcription initiation factor TFIID subunit 3
Cysteine 911 of Transcription initiation factor TFIID subunit 3
5xmy C 870 C 873
A redox-regulated disulphide may form within Transcription initiation factor TFIID subunit 3 between cysteines 868 and 871 (870 and 873 respectively in this structure).
Details
Redox score ?
85
PDB code
5xmy
Structure name
crystal structure of taf3 phd finger bound to h3k4me3q5ser
Structure deposition date
2017-05-16
Thiol separation (Å)
3
Half-sphere exposure sum ?
50
Minimum pKa ?
7
% buried
14
Peptide accession
Q5VWG9
Residue number A
868
Residue number B
871
Peptide name
Transcription initiation factor TFIID subunit 3
Ligandability
Cysteine 868 of Transcription initiation factor TFIID subunit 3
Cysteine 871 of Transcription initiation factor TFIID subunit 3
2k17 A 888 A 911
A redox-regulated disulphide may form within Transcription initiation factor TFIID subunit 3 between cysteines 888 and 911.
Details
Redox score ?
84
PDB code
2k17
Structure name
solution structure of the taf3 phd domain in complex with a h3k4me3 peptide
Structure deposition date
2008-02-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
23
Peptide accession
Q5HZG4
Residue number A
888
Residue number B
911
Peptide name
Transcription initiation factor TFIID subunit 3
Ligandability
Cysteine 888 of Transcription initiation factor TFIID subunit 3
Cysteine 911 of Transcription initiation factor TFIID subunit 3
2k16 A 911 A 914
A redox-regulated disulphide may form within Transcription initiation factor TFIID subunit 3 between cysteines 911 and 914.
Details
Redox score ?
83
PDB code
2k16
Structure name
solution structure of the free taf3 phd domain
Structure deposition date
2008-02-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
7
% buried
10
Peptide accession
Q5HZG4
Residue number A
911
Residue number B
914
Peptide name
Transcription initiation factor TFIID subunit 3
Ligandability
Cysteine 911 of Transcription initiation factor TFIID subunit 3
Cysteine 914 of Transcription initiation factor TFIID subunit 3
5c13 E 870 E 896
A redox-regulated disulphide may form within Transcription initiation factor TFIID subunit 3 between cysteines 868 and 894 (870 and 896 respectively in this structure).
Details
Redox score ?
82
PDB code
5c13
Structure name
crystal structure of taf3 phd finger bound to histone h3c4me3 peptide
Structure deposition date
2015-06-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
7
% buried
22
Peptide accession
Q5VWG9
Residue number A
868
Residue number B
894
Peptide name
Transcription initiation factor TFIID subunit 3
Ligandability
Cysteine 868 of Transcription initiation factor TFIID subunit 3
Cysteine 894 of Transcription initiation factor TFIID subunit 3
2k16 A 888 A 914
A redox-regulated disulphide may form within Transcription initiation factor TFIID subunit 3 between cysteines 888 and 914.
Details
Redox score ?
78
PDB code
2k16
Structure name
solution structure of the free taf3 phd domain
Structure deposition date
2008-02-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
10
% buried
5
Peptide accession
Q5HZG4
Residue number A
888
Residue number B
914
Peptide name
Transcription initiation factor TFIID subunit 3
Ligandability
Cysteine 888 of Transcription initiation factor TFIID subunit 3
Cysteine 914 of Transcription initiation factor TFIID subunit 3
5c13 C 873 C 896
A redox-regulated disulphide may form within Transcription initiation factor TFIID subunit 3 between cysteines 871 and 894 (873 and 896 respectively in this structure).
Details
Redox score ?
71
PDB code
5c13
Structure name
crystal structure of taf3 phd finger bound to histone h3c4me3 peptide
Structure deposition date
2015-06-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
44
Peptide accession
Q5VWG9
Residue number A
871
Residue number B
894
Peptide name
Transcription initiation factor TFIID subunit 3
Ligandability
Cysteine 871 of Transcription initiation factor TFIID subunit 3
Cysteine 894 of Transcription initiation factor TFIID subunit 3
2k17 A 870 A 911
A redox-regulated disulphide may form within Transcription initiation factor TFIID subunit 3 between cysteines 870 and 911. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
2k17
Structure name
solution structure of the taf3 phd domain in complex with a h3k4me3 peptide
Structure deposition date
2008-02-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
6
% buried
30
Peptide accession
Q5HZG4
Residue number A
870
Residue number B
911
Peptide name
Transcription initiation factor TFIID subunit 3
Ligandability
Cysteine 870 of Transcription initiation factor TFIID subunit 3
Cysteine 911 of Transcription initiation factor TFIID subunit 3
2k16 A 870 A 885
A redox-regulated disulphide may form within Transcription initiation factor TFIID subunit 3 between cysteines 870 and 885. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
2k16
Structure name
solution structure of the free taf3 phd domain
Structure deposition date
2008-02-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
6
% buried
18
Peptide accession
Q5HZG4
Residue number A
870
Residue number B
885
Peptide name
Transcription initiation factor TFIID subunit 3
Ligandability
Cysteine 870 of Transcription initiation factor TFIID subunit 3
Cysteine 885 of Transcription initiation factor TFIID subunit 3
2k16 A 870 A 888
A redox-regulated disulphide may form within Transcription initiation factor TFIID subunit 3 between cysteines 870 and 888. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
2k16
Structure name
solution structure of the free taf3 phd domain
Structure deposition date
2008-02-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
17
Peptide accession
Q5HZG4
Residue number A
870
Residue number B
888
Peptide name
Transcription initiation factor TFIID subunit 3
Ligandability
Cysteine 870 of Transcription initiation factor TFIID subunit 3
Cysteine 888 of Transcription initiation factor TFIID subunit 3
7eg9 c 18 c 31
A redox-regulated disulphide may form within Transcription initiation factor TFIID subunit 3 between cysteines 18 and 31. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
7eg9
Structure name
tfiid-based intermediate pic on scp promoter
Structure deposition date
2021-03-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
11
% buried
100
Peptide accession
Q5VWG9
Residue number A
18
Residue number B
31
Peptide name
Transcription initiation factor TFIID subunit 3
Ligandability
Cysteine 18 of Transcription initiation factor TFIID subunit 3
Cysteine 31 of Transcription initiation factor TFIID subunit 3
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