Transcription elongation factor A protein 1
Intermolecular
Cysteine 641 of DNA-directed RNA polymerase II subunit RPB1 and cysteine 301
Intramolecular
Cysteine 263 and cysteine 266 L
Cysteine 263 and cysteine 291 L
Cysteine 263 and cysteine 294 L
Cysteine 266 and cysteine 291
Cysteine 291 and cysteine 294
Cysteine 271 and cysteine 291 L
Cysteine 263 and cysteine 271 L
Cysteine 266 and cysteine 294
Cysteine 266 and cysteine 271 L
Cysteine 271 and cysteine 294 L
6o9l A 641 U 301
A redox-regulated disulphide may form between cysteine 641 of DNA-directed RNA polymerase II subunit RPB1 and cysteine 301 of Transcription elongation factor A protein 1.
Details
Redox score ?
67
PDB code
6o9l
Structure name
human holo-pic in the closed state
Structure deposition date
2019-03-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
89
Peptide A name
DNA-directed RNA polymerase II subunit RPB1
Peptide B name
Transcription elongation factor A protein 1
Peptide A accession
P24928
Peptide B accession
P23193
Peptide A residue number
641
Peptide B residue number
301
Ligandability
Cysteine 641 of DNA-directed RNA polymerase II subunit RPB1
Cysteine 301 of Transcription elongation factor A protein 1
1tfi A 12 A 15
A redox-regulated disulphide may form within Transcription elongation factor A protein 1 between cysteines 263 and 266 (12 and 15 respectively in this structure).
Details
Redox score ?
89
PDB code
1tfi
Structure name
a novel zn finger motif in the basal transcriptional machinery: three- dimensional nmr studies of the nucleic-acid binding domain of transcriptional elongation factor tfiis
Structure deposition date
1993-04-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
6
% buried
0
Peptide accession
P23193
Residue number A
263
Residue number B
266
Peptide name
Transcription elongation factor A protein 1
Ligandability
Cysteine 263 of Transcription elongation factor A protein 1
Cysteine 266 of Transcription elongation factor A protein 1
1tfi A 12 A 40
A redox-regulated disulphide may form within Transcription elongation factor A protein 1 between cysteines 263 and 291 (12 and 40 respectively in this structure).
Details
Redox score ?
89
PDB code
1tfi
Structure name
a novel zn finger motif in the basal transcriptional machinery: three- dimensional nmr studies of the nucleic-acid binding domain of transcriptional elongation factor tfiis
Structure deposition date
1993-04-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
6
% buried
0
Peptide accession
P23193
Residue number A
263
Residue number B
291
Peptide name
Transcription elongation factor A protein 1
Ligandability
Cysteine 263 of Transcription elongation factor A protein 1
Cysteine 291 of Transcription elongation factor A protein 1
1tfi A 12 A 43
A redox-regulated disulphide may form within Transcription elongation factor A protein 1 between cysteines 263 and 294 (12 and 43 respectively in this structure).
Details
Redox score ?
88
PDB code
1tfi
Structure name
a novel zn finger motif in the basal transcriptional machinery: three- dimensional nmr studies of the nucleic-acid binding domain of transcriptional elongation factor tfiis
Structure deposition date
1993-04-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
6
% buried
0
Peptide accession
P23193
Residue number A
263
Residue number B
294
Peptide name
Transcription elongation factor A protein 1
Ligandability
Cysteine 263 of Transcription elongation factor A protein 1
Cysteine 294 of Transcription elongation factor A protein 1
1tfi A 15 A 40
A redox-regulated disulphide may form within Transcription elongation factor A protein 1 between cysteines 266 and 291 (15 and 40 respectively in this structure).
Details
Redox score ?
83
PDB code
1tfi
Structure name
a novel zn finger motif in the basal transcriptional machinery: three- dimensional nmr studies of the nucleic-acid binding domain of transcriptional elongation factor tfiis
Structure deposition date
1993-04-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
6
% buried
0
Peptide accession
P23193
Residue number A
266
Residue number B
291
Peptide name
Transcription elongation factor A protein 1
Ligandability
Cysteine 266 of Transcription elongation factor A protein 1
Cysteine 291 of Transcription elongation factor A protein 1
1tfi A 40 A 43
A redox-regulated disulphide may form within Transcription elongation factor A protein 1 between cysteines 291 and 294 (40 and 43 respectively in this structure).
Details
Redox score ?
82
PDB code
1tfi
Structure name
a novel zn finger motif in the basal transcriptional machinery: three- dimensional nmr studies of the nucleic-acid binding domain of transcriptional elongation factor tfiis
Structure deposition date
1993-04-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
0
Peptide accession
P23193
Residue number A
291
Residue number B
294
Peptide name
Transcription elongation factor A protein 1
Ligandability
Cysteine 291 of Transcription elongation factor A protein 1
Cysteine 294 of Transcription elongation factor A protein 1
1tfi A 20 A 40
A redox-regulated disulphide may form within Transcription elongation factor A protein 1 between cysteines 271 and 291 (20 and 40 respectively in this structure).
Details
Redox score ?
78
PDB code
1tfi
Structure name
a novel zn finger motif in the basal transcriptional machinery: three- dimensional nmr studies of the nucleic-acid binding domain of transcriptional elongation factor tfiis
Structure deposition date
1993-04-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
61
Minimum pKa ?
6
% buried
0
Peptide accession
P23193
Residue number A
271
Residue number B
291
Peptide name
Transcription elongation factor A protein 1
Ligandability
Cysteine 271 of Transcription elongation factor A protein 1
Cysteine 291 of Transcription elongation factor A protein 1
1tfi A 12 A 20
A redox-regulated disulphide may form within Transcription elongation factor A protein 1 between cysteines 263 and 271 (12 and 20 respectively in this structure).
Details
Redox score ?
78
PDB code
1tfi
Structure name
a novel zn finger motif in the basal transcriptional machinery: three- dimensional nmr studies of the nucleic-acid binding domain of transcriptional elongation factor tfiis
Structure deposition date
1993-04-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
0
Peptide accession
P23193
Residue number A
263
Residue number B
271
Peptide name
Transcription elongation factor A protein 1
Ligandability
Cysteine 263 of Transcription elongation factor A protein 1
Cysteine 271 of Transcription elongation factor A protein 1
1tfi A 15 A 43
A redox-regulated disulphide may form within Transcription elongation factor A protein 1 between cysteines 266 and 294 (15 and 43 respectively in this structure).
Details
Redox score ?
77
PDB code
1tfi
Structure name
a novel zn finger motif in the basal transcriptional machinery: three- dimensional nmr studies of the nucleic-acid binding domain of transcriptional elongation factor tfiis
Structure deposition date
1993-04-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
33
Minimum pKa ?
10
% buried
0
Peptide accession
P23193
Residue number A
266
Residue number B
294
Peptide name
Transcription elongation factor A protein 1
Ligandability
Cysteine 266 of Transcription elongation factor A protein 1
Cysteine 294 of Transcription elongation factor A protein 1
1tfi A 15 A 20
A redox-regulated disulphide may form within Transcription elongation factor A protein 1 between cysteines 266 and 271 (15 and 20 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
1tfi
Structure name
a novel zn finger motif in the basal transcriptional machinery: three- dimensional nmr studies of the nucleic-acid binding domain of transcriptional elongation factor tfiis
Structure deposition date
1993-04-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
46
Minimum pKa ?
11
% buried
0
Peptide accession
P23193
Residue number A
266
Residue number B
271
Peptide name
Transcription elongation factor A protein 1
Ligandability
Cysteine 266 of Transcription elongation factor A protein 1
Cysteine 271 of Transcription elongation factor A protein 1
1tfi A 20 A 43
A redox-regulated disulphide may form within Transcription elongation factor A protein 1 between cysteines 271 and 294 (20 and 43 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
1tfi
Structure name
a novel zn finger motif in the basal transcriptional machinery: three- dimensional nmr studies of the nucleic-acid binding domain of transcriptional elongation factor tfiis
Structure deposition date
1993-04-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
47
Minimum pKa ?
10
% buried
0
Peptide accession
P23193
Residue number A
271
Residue number B
294
Peptide name
Transcription elongation factor A protein 1
Ligandability
Cysteine 271 of Transcription elongation factor A protein 1
Cysteine 294 of Transcription elongation factor A protein 1
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