ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Transcription elongation factor SPT4

Intramolecular
Cysteine 33 and cysteine 36 L
Cysteine 19 and cysteine 36 L
Cysteine 16 and cysteine 36 L
Cysteine 19 and cysteine 33 L
Cysteine 16 and cysteine 33 L
Cysteine 16 and cysteine 19
Cysteine 16 and cysteine 52
Cysteine 33 and cysteine 52 L
Cysteine 36 and cysteine 52 L
Cysteine 19 and cysteine 52
A redox-regulated disulphide may form within Transcription elongation factor SPT4 between cysteines 33 and 36.

Details

Redox score ?
76
PDB code
3h7h
Structure name
crystal structure of the human transcription elongation factor dsif, hspt4/hspt5 (176-273)
Structure deposition date
2009-04-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
6
% buried
91
Peptide accession
P63272
Residue number A
33
Residue number B
36
Peptide name
Transcription elongation factor SPT4

Ligandability

Cysteine 33 of Transcription elongation factor SPT4

Cysteine 36 of Transcription elongation factor SPT4

A redox-regulated disulphide may form within Transcription elongation factor SPT4 between cysteines 19 and 36.

Details

Redox score ?
76
PDB code
3h7h
Structure name
crystal structure of the human transcription elongation factor dsif, hspt4/hspt5 (176-273)
Structure deposition date
2009-04-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
5
% buried
91
Peptide accession
P63272
Residue number A
19
Residue number B
36
Peptide name
Transcription elongation factor SPT4

Ligandability

Cysteine 19 of Transcription elongation factor SPT4

Cysteine 36 of Transcription elongation factor SPT4

A redox-regulated disulphide may form within Transcription elongation factor SPT4 between cysteines 16 and 36.

Details

Redox score ?
75
PDB code
3h7h
Structure name
crystal structure of the human transcription elongation factor dsif, hspt4/hspt5 (176-273)
Structure deposition date
2009-04-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
5
% buried
91
Peptide accession
P63272
Residue number A
16
Residue number B
36
Peptide name
Transcription elongation factor SPT4

Ligandability

Cysteine 16 of Transcription elongation factor SPT4

Cysteine 36 of Transcription elongation factor SPT4

A redox-regulated disulphide may form within Transcription elongation factor SPT4 between cysteines 19 and 33.

Details

Redox score ?
75
PDB code
3h7h
Structure name
crystal structure of the human transcription elongation factor dsif, hspt4/hspt5 (176-273)
Structure deposition date
2009-04-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
87
Minimum pKa ?
5
% buried
100
Peptide accession
P63272
Residue number A
19
Residue number B
33
Peptide name
Transcription elongation factor SPT4

Ligandability

Cysteine 19 of Transcription elongation factor SPT4

Cysteine 33 of Transcription elongation factor SPT4

A redox-regulated disulphide may form within Transcription elongation factor SPT4 between cysteines 16 and 33.

Details

Redox score ?
72
PDB code
3h7h
Structure name
crystal structure of the human transcription elongation factor dsif, hspt4/hspt5 (176-273)
Structure deposition date
2009-04-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
89
Minimum pKa ?
5
% buried
100
Peptide accession
P63272
Residue number A
16
Residue number B
33
Peptide name
Transcription elongation factor SPT4

Ligandability

Cysteine 16 of Transcription elongation factor SPT4

Cysteine 33 of Transcription elongation factor SPT4

A redox-regulated disulphide may form within Transcription elongation factor SPT4 between cysteines 16 and 19.

Details

Redox score ?
71
PDB code
3h7h
Structure name
crystal structure of the human transcription elongation factor dsif, hspt4/hspt5 (176-273)
Structure deposition date
2009-04-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
88
Minimum pKa ?
5
% buried
100
Peptide accession
P63272
Residue number A
16
Residue number B
19
Peptide name
Transcription elongation factor SPT4

Ligandability

Cysteine 16 of Transcription elongation factor SPT4

Cysteine 19 of Transcription elongation factor SPT4

A redox-regulated disulphide may form within Transcription elongation factor SPT4 between cysteines 16 and 52. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
3h7h
Structure name
crystal structure of the human transcription elongation factor dsif, hspt4/hspt5 (176-273)
Structure deposition date
2009-04-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
86
Minimum pKa ?
5
% buried
82
Peptide accession
P63272
Residue number A
16
Residue number B
52
Peptide name
Transcription elongation factor SPT4

Ligandability

Cysteine 16 of Transcription elongation factor SPT4

Cysteine 52 of Transcription elongation factor SPT4

A redox-regulated disulphide may form within Transcription elongation factor SPT4 between cysteines 33 and 52. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
3h7h
Structure name
crystal structure of the human transcription elongation factor dsif, hspt4/hspt5 (176-273)
Structure deposition date
2009-04-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
6
% buried
82
Peptide accession
P63272
Residue number A
33
Residue number B
52
Peptide name
Transcription elongation factor SPT4

Ligandability

Cysteine 33 of Transcription elongation factor SPT4

Cysteine 52 of Transcription elongation factor SPT4

A redox-regulated disulphide may form within Transcription elongation factor SPT4 between cysteines 36 and 52. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3h7h
Structure name
crystal structure of the human transcription elongation factor dsif, hspt4/hspt5 (176-273)
Structure deposition date
2009-04-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
12
% buried
73
Peptide accession
P63272
Residue number A
36
Residue number B
52
Peptide name
Transcription elongation factor SPT4

Ligandability

Cysteine 36 of Transcription elongation factor SPT4

Cysteine 52 of Transcription elongation factor SPT4

A redox-regulated disulphide may form within Transcription elongation factor SPT4 between cysteines 19 and 52. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
6ted
Structure name
structure of complete, activated transcription complex pol ii-dsif- paf-spt6 uncovers allosteric elongation activation by rtf1
Structure deposition date
2019-11-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
86
Peptide accession
P63272
Residue number A
19
Residue number B
52
Peptide name
Transcription elongation factor SPT4

Ligandability

Cysteine 19 of Transcription elongation factor SPT4

Cysteine 52 of Transcription elongation factor SPT4

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