ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Elongator complex protein 1

Intramolecular
Cysteine 562 and cysteine 563
Cysteine 370 and cysteine 371
Cysteine 23 and cysteine 70
Cysteine 953 and cysteine 961
Cysteine 563 and cysteine 564
Cysteine 562 and cysteine 564
Cysteine 84 and cysteine 95
Cysteine 23 and cysteine 25
A redox-regulated disulphide may form within Elongator complex protein 1 between cysteines 562 and 563. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
8avg
Structure name
cryo-em structure of mouse elp123 with bound sam
Structure deposition date
2022-08-26
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
92
Peptide accession
Q7TT37
Residue number A
562
Residue number B
563
Peptide name
Elongator complex protein 1

Ligandability

Cysteine 562 of Elongator complex protein 1

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 563 of Elongator complex protein 1

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 Elongator complex protein 1 between cysteines 370 and 371. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
8avg
Structure name
cryo-em structure of mouse elp123 with bound sam
Structure deposition date
2022-08-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
56
Minimum pKa ?
11
% buried
82
Peptide accession
Q7TT37
Residue number A
370
Residue number B
371
Peptide name
Elongator complex protein 1

Ligandability

Cysteine 370 of Elongator complex protein 1

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 Elongator complex protein 1

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 Elongator complex protein 1 between cysteines 23 and 70. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
8avg
Structure name
cryo-em structure of mouse elp123 with bound sam
Structure deposition date
2022-08-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
56
Peptide accession
Q7TT37
Residue number A
23
Residue number B
70
Peptide name
Elongator complex protein 1

Ligandability

Cysteine 23 of Elongator complex protein 1

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 70 of Elongator complex protein 1

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 Elongator complex protein 1 between cysteines 953 and 961. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
5cqr
Structure name
dimerization of elp1 is essential for elongator complex assembly
Structure deposition date
2015-07-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
11
% buried
40
Peptide accession
O95163
Residue number A
953
Residue number B
961
Peptide name
Elongator complex protein 1

Ligandability

Cysteine 953 of Elongator complex protein 1

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 961 of Elongator complex protein 1

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 Elongator complex protein 1 between cysteines 563 and 564. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
8avg
Structure name
cryo-em structure of mouse elp123 with bound sam
Structure deposition date
2022-08-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
86
Peptide accession
Q7TT37
Residue number A
563
Residue number B
564
Peptide name
Elongator complex protein 1

Ligandability

Cysteine 563 of Elongator complex protein 1

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 564 of Elongator complex protein 1

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 Elongator complex protein 1 between cysteines 562 and 564. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
8avg
Structure name
cryo-em structure of mouse elp123 with bound sam
Structure deposition date
2022-08-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
78
Peptide accession
Q7TT37
Residue number A
562
Residue number B
564
Peptide name
Elongator complex protein 1

Ligandability

Cysteine 562 of Elongator complex protein 1

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 564 of Elongator complex protein 1

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 Elongator complex protein 1 between cysteines 84 and 95. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
8avg
Structure name
cryo-em structure of mouse elp123 with bound sam
Structure deposition date
2022-08-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
59
Peptide accession
Q7TT37
Residue number A
84
Residue number B
95
Peptide name
Elongator complex protein 1

Ligandability

Cysteine 84 of Elongator complex protein 1

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 95 of Elongator complex protein 1

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 Elongator complex protein 1 between cysteines 23 and 25. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
8avg
Structure name
cryo-em structure of mouse elp123 with bound sam
Structure deposition date
2022-08-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
83
Peptide accession
Q7TT37
Residue number A
23
Residue number B
25
Peptide name
Elongator complex protein 1

Ligandability

Cysteine 23 of Elongator complex protein 1

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 25 of Elongator complex protein 1

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.

If this tool was useful for finding a disulphide, please cite: