ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Telomerase-binding protein EST1A

Intramolecular
Cysteine 1065 and cysteine 1139
Cysteine 1359 and cysteine 1360
Cysteine 1360 and cysteine 1364
Cysteine 728 and cysteine 731
Cysteine 986 and cysteine 988
Cysteine 1111 and cysteine 1125
A redox-regulated disulphide may form within Telomerase-binding protein EST1A between cysteines 1065 and 1139.

Details

Redox score ?
62
PDB code
4um2
Structure name
crystal structure of the tpr domain of smg6
Structure deposition date
2014-05-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
48
Peptide accession
Q86US8
Residue number A
1065
Residue number B
1139
Peptide name
Telomerase-binding protein EST1A

Ligandability

Cysteine 1065 of Telomerase-binding protein EST1A

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 1139 of Telomerase-binding protein EST1A

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 Telomerase-binding protein EST1A between cysteines 1359 and 1360 (126 and 127 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2dok
Structure name
crystal structure of the pin domain of human est1a
Structure deposition date
2006-05-01
Thiol separation (Å)
6
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
96
Peptide accession
Q86US8
Residue number A
1359
Residue number B
1360
Peptide name
Telomerase-binding protein EST1A

Ligandability

Cysteine 1359 of Telomerase-binding protein EST1A

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 1360 of Telomerase-binding protein EST1A

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 Telomerase-binding protein EST1A between cysteines 1360 and 1364 (127 and 131 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2dok
Structure name
crystal structure of the pin domain of human est1a
Structure deposition date
2006-05-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
82
Peptide accession
Q86US8
Residue number A
1360
Residue number B
1364
Peptide name
Telomerase-binding protein EST1A

Ligandability

Cysteine 1360 of Telomerase-binding protein EST1A

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 1364 of Telomerase-binding protein EST1A

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 Telomerase-binding protein EST1A between cysteines 728 and 731. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
4um2
Structure name
crystal structure of the tpr domain of smg6
Structure deposition date
2014-05-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
80
Minimum pKa ?
13
% buried
100
Peptide accession
Q86US8
Residue number A
728
Residue number B
731
Peptide name
Telomerase-binding protein EST1A

Ligandability

Cysteine 728 of Telomerase-binding protein EST1A

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 731 of Telomerase-binding protein EST1A

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 Telomerase-binding protein EST1A between cysteines 986 and 988. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
4um2
Structure name
crystal structure of the tpr domain of smg6
Structure deposition date
2014-05-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
64
Peptide accession
Q86US8
Residue number A
986
Residue number B
988
Peptide name
Telomerase-binding protein EST1A

Ligandability

Cysteine 986 of Telomerase-binding protein EST1A

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 988 of Telomerase-binding protein EST1A

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 Telomerase-binding protein EST1A between cysteines 1111 and 1125. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
4um2
Structure name
crystal structure of the tpr domain of smg6
Structure deposition date
2014-05-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
45
Peptide accession
Q86US8
Residue number A
1111
Residue number B
1125
Peptide name
Telomerase-binding protein EST1A

Ligandability

Cysteine 1111 of Telomerase-binding protein EST1A

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 1125 of Telomerase-binding protein EST1A

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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