Transcription initiation factor IIB
Intermolecular
Cysteine 223 and cysteine 223 L
Intramolecular
Cysteine 15 and cysteine 34
Cysteine 15 and cysteine 37
Cysteine 34 and cysteine 37
Cysteine 163 and cysteine 168
Cysteine 168 and cysteine 181
Cysteine 181 and cysteine 194
Cysteine 163 and cysteine 194
5wh1 A 223 C 223
A redox-regulated disulphide may form between two units of Transcription initiation factor IIB at cysteines 223 and 223.
Details
Redox score ?
67
PDB code
5wh1
Structure name
apo form of the c-terminal region of human transcription factor iib
Structure deposition date
2017-07-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
91
Minimum pKa ?
6
% buried
100
Peptide A name
Transcription initiation factor IIB
Peptide B name
Transcription initiation factor IIB
Peptide A accession
Q00403
Peptide B accession
Q00403
Peptide A residue number
223
Peptide B residue number
223
Ligandability
1dl6 A 15 A 34
A redox-regulated disulphide may form within Transcription initiation factor IIB between cysteines 15 and 34.
Details
Redox score ?
89
PDB code
1dl6
Structure name
solution structure of human tfiib n-terminal domain
Structure deposition date
1999-12-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
0
Peptide accession
Q00403
Residue number A
15
Residue number B
34
Peptide name
Transcription initiation factor IIB
Ligandability
Cysteine 15 of Transcription initiation factor IIB
Cysteine 34 of Transcription initiation factor IIB
1rly A 15 A 37
A redox-regulated disulphide may form within Transcription initiation factor IIB between cysteines 15 and 37.
Details
Redox score ?
82
PDB code
1rly
Structure name
rdc-derived models of the zinc ribbon domain of human general transcription tfiib (zinc bound structures)
Structure deposition date
2003-11-26
Thiol separation (Å)
3
Half-sphere exposure sum ?
42
Minimum pKa ?
8
% buried
nan
Peptide accession
Q00403
Residue number A
15
Residue number B
37
Peptide name
Transcription initiation factor IIB
Ligandability
Cysteine 15 of Transcription initiation factor IIB
Cysteine 37 of Transcription initiation factor IIB
1rly A 34 A 37
A redox-regulated disulphide may form within Transcription initiation factor IIB between cysteines 34 and 37.
Details
Redox score ?
76
PDB code
1rly
Structure name
rdc-derived models of the zinc ribbon domain of human general transcription tfiib (zinc bound structures)
Structure deposition date
2003-11-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
nan
Peptide accession
Q00403
Residue number A
34
Residue number B
37
Peptide name
Transcription initiation factor IIB
Ligandability
Cysteine 34 of Transcription initiation factor IIB
Cysteine 37 of Transcription initiation factor IIB
2phg A 163 A 168
A redox-regulated disulphide may form within Transcription initiation factor IIB between cysteines 163 and 168. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
2phg
Structure name
model for vp16 binding to tfiib
Structure deposition date
2007-04-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
94
Peptide accession
Q00403
Residue number A
163
Residue number B
168
Peptide name
Transcription initiation factor IIB
Ligandability
Cysteine 163 of Transcription initiation factor IIB
Cysteine 168 of Transcription initiation factor IIB
2phg A 168 A 181
A redox-regulated disulphide may form within Transcription initiation factor IIB between cysteines 168 and 181. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
2phg
Structure name
model for vp16 binding to tfiib
Structure deposition date
2007-04-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
84
Peptide accession
Q00403
Residue number A
168
Residue number B
181
Peptide name
Transcription initiation factor IIB
Ligandability
Cysteine 168 of Transcription initiation factor IIB
Cysteine 181 of Transcription initiation factor IIB
1tfb A 181 A 194
A redox-regulated disulphide may form within Transcription initiation factor IIB between cysteines 181 and 194. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
1tfb
Structure name
nmr studies of human general transcription factor tfiib: dynamics and interaction with vp16 activation domain, 20 structures
Structure deposition date
1996-11-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
54
Peptide accession
Q00403
Residue number A
181
Residue number B
194
Peptide name
Transcription initiation factor IIB
Ligandability
Cysteine 181 of Transcription initiation factor IIB
Cysteine 194 of Transcription initiation factor IIB
1c9b A 163 A 194
A redox-regulated disulphide may form within Transcription initiation factor IIB between cysteines 163 and 194. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
1c9b
Structure name
crystal structure of a human tbp core domain-human tfiib core domain complex bound to an extended, modified adenoviral major late promoter (admlp)
Structure deposition date
1999-08-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
13
% buried
98
Peptide accession
Q00403
Residue number A
163
Residue number B
194
Peptide name
Transcription initiation factor IIB
Ligandability
Cysteine 163 of Transcription initiation factor IIB
Cysteine 194 of Transcription initiation factor IIB
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