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General transcription factor IIH subunit 3

Intermolecular
Cysteine 142 and cysteine 371 of General transcription factor IIH subunit 2
Cysteine 285 and cysteine 247 of General transcription factor IIH subunit 2
Cysteine 142 and cysteine 345 of General transcription factor IIH subunit 2
Cysteine 142 and cysteine 348 of General transcription factor IIH subunit 2
Cysteine 268 and cysteine 247 of General transcription factor IIH subunit 2
Cysteine 282 and cysteine 247 of General transcription factor IIH subunit 2
Cysteine 142 and cysteine 368 of General transcription factor IIH subunit 2
Cysteine 271 and cysteine 247 of General transcription factor IIH subunit 2
Cysteine 142 and cysteine 381 of General transcription factor IIH subunit 2
Cysteine 142 and cysteine 382 of General transcription factor IIH subunit 2
More...
Intramolecular
Cysteine 268 and cysteine 282
Cysteine 282 and cysteine 285
Cysteine 271 and cysteine 282
Cysteine 268 and cysteine 271
Cysteine 257 and cysteine 276
Cysteine 255 and cysteine 257
Cysteine 271 and cysteine 285
Cysteine 268 and cysteine 285
Cysteine 257 and cysteine 268
Cysteine 255 and cysteine 276
Cysteine 257 and cysteine 285
Cysteine 268 and cysteine 276
Cysteine 37 and cysteine 194
Cysteine 194 and cysteine 207
A redox-regulated disulphide may form between cysteine 142 of General transcription factor IIH subunit 3 and cysteine 371 of General transcription factor IIH subunit 2.

Details

Redox score ?
71
PDB code
5o85
Structure name
p34-p44 complex
Structure deposition date
2017-06-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
9
% buried
86
Peptide A name
General transcription factor IIH subunit 3
Peptide B name
General transcription factor IIH subunit 2
Peptide A accession
Q13889
Peptide B accession
Q13888
Peptide A residue number
142
Peptide B residue number
371

Ligandability

Cysteine 142 of General transcription factor IIH subunit 3

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 371 of General transcription factor IIH subunit 2

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 between cysteine 285 of General transcription factor IIH subunit 3 and cysteine 247 of General transcription factor IIH subunit 2.

Details

Redox score ?
67
PDB code
7nw0
Structure name
rna polymerase ii pre-initiation complex with open promoter dna
Structure deposition date
2021-03-16
Thiol separation (Å)
5
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
62
Peptide A name
General transcription factor IIH subunit 3
Peptide B name
General transcription factor IIH subunit 2
Peptide A accession
Q13889
Peptide B accession
Q13888
Peptide A residue number
285
Peptide B residue number
247

Ligandability

Cysteine 285 of General transcription factor IIH subunit 3

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 247 of General transcription factor IIH subunit 2

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 between cysteine 142 of General transcription factor IIH subunit 3 and cysteine 345 of General transcription factor IIH subunit 2.

Details

Redox score ?
61
PDB code
5o85
Structure name
p34-p44 complex
Structure deposition date
2017-06-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
nan
Peptide A name
General transcription factor IIH subunit 3
Peptide B name
General transcription factor IIH subunit 2
Peptide A accession
Q13889
Peptide B accession
Q13888
Peptide A residue number
142
Peptide B residue number
345

Ligandability

Cysteine 142 of General transcription factor IIH subunit 3

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 345 of General transcription factor IIH subunit 2

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 between cysteine 142 of General transcription factor IIH subunit 3 and cysteine 348 of General transcription factor IIH subunit 2.

Details

Redox score ?
61
PDB code
5o85
Structure name
p34-p44 complex
Structure deposition date
2017-06-12
Thiol separation (Å)
5
Half-sphere exposure sum ?
83
Minimum pKa ?
9
% buried
76
Peptide A name
General transcription factor IIH subunit 3
Peptide B name
General transcription factor IIH subunit 2
Peptide A accession
Q13889
Peptide B accession
Q13888
Peptide A residue number
142
Peptide B residue number
348

Ligandability

Cysteine 142 of General transcription factor IIH subunit 3

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 348 of General transcription factor IIH subunit 2

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 between cysteine 268 of General transcription factor IIH subunit 3 and cysteine 247 of General transcription factor IIH subunit 2. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
6o9m
Structure name
structure of the human apo tfiih
Structure deposition date
2019-03-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
5
% buried
64
Peptide A name
General transcription factor IIH subunit 3
Peptide B name
General transcription factor IIH subunit 2
Peptide A accession
Q13889
Peptide B accession
Q13888
Peptide A residue number
268
Peptide B residue number
247

Ligandability

Cysteine 268 of General transcription factor IIH subunit 3

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 247 of General transcription factor IIH subunit 2

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 between cysteine 282 of General transcription factor IIH subunit 3 and cysteine 247 of General transcription factor IIH subunit 2. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
7nw0
Structure name
rna polymerase ii pre-initiation complex with open promoter dna
Structure deposition date
2021-03-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
9
% buried
60
Peptide A name
General transcription factor IIH subunit 3
Peptide B name
General transcription factor IIH subunit 2
Peptide A accession
Q13889
Peptide B accession
Q13888
Peptide A residue number
282
Peptide B residue number
247

Ligandability

Cysteine 282 of General transcription factor IIH subunit 3

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 247 of General transcription factor IIH subunit 2

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 between cysteine 142 of General transcription factor IIH subunit 3 and cysteine 368 of General transcription factor IIH subunit 2. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
5o85
Structure name
p34-p44 complex
Structure deposition date
2017-06-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
70
Peptide A name
General transcription factor IIH subunit 3
Peptide B name
General transcription factor IIH subunit 2
Peptide A accession
Q13889
Peptide B accession
Q13888
Peptide A residue number
142
Peptide B residue number
368

Ligandability

Cysteine 142 of General transcription factor IIH subunit 3

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 368 of General transcription factor IIH subunit 2

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 between cysteine 271 of General transcription factor IIH subunit 3 and cysteine 247 of General transcription factor IIH subunit 2. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
7nvz
Structure name
rna polymerase ii pre-initiation complex with closed promoter dna in distal position
Structure deposition date
2021-03-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
6
% buried
66
Peptide A name
General transcription factor IIH subunit 3
Peptide B name
General transcription factor IIH subunit 2
Peptide A accession
Q13889
Peptide B accession
Q13888
Peptide A residue number
271
Peptide B residue number
247

Ligandability

Cysteine 271 of General transcription factor IIH subunit 3

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 247 of General transcription factor IIH subunit 2

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 between cysteine 142 of General transcription factor IIH subunit 3 and cysteine 381 of General transcription factor IIH subunit 2. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6o9l
Structure name
human holo-pic in the closed state
Structure deposition date
2019-03-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
8
% buried
100
Peptide A name
General transcription factor IIH subunit 3
Peptide B name
General transcription factor IIH subunit 2
Peptide A accession
Q13889
Peptide B accession
Q13888
Peptide A residue number
142
Peptide B residue number
381

Ligandability

Cysteine 142 of General transcription factor IIH subunit 3

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 381 of General transcription factor IIH subunit 2

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 between cysteine 142 of General transcription factor IIH subunit 3 and cysteine 382 of General transcription factor IIH subunit 2. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
5o85
Structure name
p34-p44 complex
Structure deposition date
2017-06-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
9
% buried
76
Peptide A name
General transcription factor IIH subunit 3
Peptide B name
General transcription factor IIH subunit 2
Peptide A accession
Q13889
Peptide B accession
Q13888
Peptide A residue number
142
Peptide B residue number
382

Ligandability

Cysteine 142 of General transcription factor IIH subunit 3

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 382 of General transcription factor IIH subunit 2

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 General transcription factor IIH subunit 3 between cysteines 268 and 282.

Details

Redox score ?
87
PDB code
6ro4
Structure name
structure of the core tfiih-xpa-dna complex
Structure deposition date
2019-05-10
Thiol separation (Å)
3
Half-sphere exposure sum ?
57
Minimum pKa ?
6
% buried
24
Peptide accession
Q13889
Residue number A
268
Residue number B
282
Peptide name
General transcription factor IIH subunit 3

Ligandability

Cysteine 268 of General transcription factor IIH subunit 3

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 282 of General transcription factor IIH subunit 3

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 General transcription factor IIH subunit 3 between cysteines 282 and 285.

Details

Redox score ?
80
PDB code
6o9m
Structure name
structure of the human apo tfiih
Structure deposition date
2019-03-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
5
% buried
52
Peptide accession
Q13889
Residue number A
282
Residue number B
285
Peptide name
General transcription factor IIH subunit 3

Ligandability

Cysteine 282 of General transcription factor IIH subunit 3

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 285 of General transcription factor IIH subunit 3

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 General transcription factor IIH subunit 3 between cysteines 271 and 282.

Details

Redox score ?
78
PDB code
7ad8
Structure name
core tfiih-xpa-dna complex with modelled p62 subunit
Structure deposition date
2020-09-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
20
Peptide accession
Q13889
Residue number A
271
Residue number B
282
Peptide name
General transcription factor IIH subunit 3

Ligandability

Cysteine 271 of General transcription factor IIH subunit 3

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 282 of General transcription factor IIH subunit 3

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 General transcription factor IIH subunit 3 between cysteines 268 and 271.

Details

Redox score ?
75
PDB code
7nvz
Structure name
rna polymerase ii pre-initiation complex with closed promoter dna in distal position
Structure deposition date
2021-03-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
80
Minimum pKa ?
6
% buried
nan
Peptide accession
Q13889
Residue number A
268
Residue number B
271
Peptide name
General transcription factor IIH subunit 3

Ligandability

Cysteine 268 of General transcription factor IIH subunit 3

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 271 of General transcription factor IIH subunit 3

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 General transcription factor IIH subunit 3 between cysteines 257 and 276.

Details

Redox score ?
74
PDB code
7nvx
Structure name
tfiih in a post-translocated state (with adp-bef3)
Structure deposition date
2021-03-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
10
Peptide accession
Q13889
Residue number A
257
Residue number B
276
Peptide name
General transcription factor IIH subunit 3

Ligandability

Cysteine 257 of General transcription factor IIH subunit 3

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 276 of General transcription factor IIH subunit 3

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 General transcription factor IIH subunit 3 between cysteines 255 and 257.

Details

Redox score ?
73
PDB code
7nw0
Structure name
rna polymerase ii pre-initiation complex with open promoter dna
Structure deposition date
2021-03-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
16
Peptide accession
Q13889
Residue number A
255
Residue number B
257
Peptide name
General transcription factor IIH subunit 3

Ligandability

Cysteine 255 of General transcription factor IIH subunit 3

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 257 of General transcription factor IIH subunit 3

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 General transcription factor IIH subunit 3 between cysteines 271 and 285.

Details

Redox score ?
71
PDB code
6o9l
Structure name
human holo-pic in the closed state
Structure deposition date
2019-03-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
9
% buried
56
Peptide accession
Q13889
Residue number A
271
Residue number B
285
Peptide name
General transcription factor IIH subunit 3

Ligandability

Cysteine 271 of General transcription factor IIH subunit 3

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 285 of General transcription factor IIH subunit 3

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 General transcription factor IIH subunit 3 between cysteines 268 and 285.

Details

Redox score ?
60
PDB code
6nmi
Structure name
cryo-em structure of the human tfiih core complex
Structure deposition date
2019-01-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
14
% buried
nan
Peptide accession
Q13889
Residue number A
268
Residue number B
285
Peptide name
General transcription factor IIH subunit 3

Ligandability

Cysteine 268 of General transcription factor IIH subunit 3

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 285 of General transcription factor IIH subunit 3

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 General transcription factor IIH subunit 3 between cysteines 257 and 268. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
6o9m
Structure name
structure of the human apo tfiih
Structure deposition date
2019-03-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
5
% buried
56
Peptide accession
Q13889
Residue number A
257
Residue number B
268
Peptide name
General transcription factor IIH subunit 3

Ligandability

Cysteine 257 of General transcription factor IIH subunit 3

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 268 of General transcription factor IIH subunit 3

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 General transcription factor IIH subunit 3 between cysteines 255 and 276. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
6o9l
Structure name
human holo-pic in the closed state
Structure deposition date
2019-03-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
42
Peptide accession
Q13889
Residue number A
255
Residue number B
276
Peptide name
General transcription factor IIH subunit 3

Ligandability

Cysteine 255 of General transcription factor IIH subunit 3

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 276 of General transcription factor IIH subunit 3

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 General transcription factor IIH subunit 3 between cysteines 257 and 285. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6o9l
Structure name
human holo-pic in the closed state
Structure deposition date
2019-03-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
48
Peptide accession
Q13889
Residue number A
257
Residue number B
285
Peptide name
General transcription factor IIH subunit 3

Ligandability

Cysteine 257 of General transcription factor IIH subunit 3

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 285 of General transcription factor IIH subunit 3

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 General transcription factor IIH subunit 3 between cysteines 268 and 276. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6o9l
Structure name
human holo-pic in the closed state
Structure deposition date
2019-03-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
9
% buried
39
Peptide accession
Q13889
Residue number A
268
Residue number B
276
Peptide name
General transcription factor IIH subunit 3

Ligandability

Cysteine 268 of General transcription factor IIH subunit 3

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 276 of General transcription factor IIH subunit 3

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 General transcription factor IIH subunit 3 between cysteines 37 and 194. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
5o85
Structure name
p34-p44 complex
Structure deposition date
2017-06-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
94
Peptide accession
Q13889
Residue number A
37
Residue number B
194
Peptide name
General transcription factor IIH subunit 3

Ligandability

Cysteine 37 of General transcription factor IIH subunit 3

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 194 of General transcription factor IIH subunit 3

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 General transcription factor IIH subunit 3 between cysteines 194 and 207. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
22
PDB code
6ro4
Structure name
structure of the core tfiih-xpa-dna complex
Structure deposition date
2019-05-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
13
% buried
100
Peptide accession
Q13889
Residue number A
194
Residue number B
207
Peptide name
General transcription factor IIH subunit 3

Ligandability

Cysteine 194 of General transcription factor IIH subunit 3

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 207 of General transcription factor IIH subunit 3

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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