ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Folliculin

Intramolecular
Cysteine 11 and cysteine 85 L
Cysteine 8 and cysteine 125
Cysteine 503 and cysteine 506
Cysteine 82 and cysteine 85 L
Cysteine 8 and cysteine 21
Cysteine 131 and cysteine 134 L
Cysteine 21 and cysteine 125
A redox-regulated disulphide may form within Folliculin between cysteines 11 and 85.

Details

Redox score ?
86
PDB code
6ulg
Structure name
cryo-em structure of the flcn-fnip2-rag-ragulator complex
Structure deposition date
2019-10-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
3
% buried
82
Peptide accession
Q8NFG4
Residue number A
11
Residue number B
85
Peptide name
Folliculin

Ligandability

Cysteine 11 of Folliculin

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 85 of Folliculin

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Folliculin between cysteines 8 and 125.

Details

Redox score ?
81
PDB code
6nzd
Structure name
cryo-em structure of the lysosomal folliculin complex (flcn-fnip2- raga-ragc-ragulator)
Structure deposition date
2019-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NFG4
Residue number A
8
Residue number B
125
Peptide name
Folliculin

Ligandability

Cysteine 8 of Folliculin

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 125 of Folliculin

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 Folliculin between cysteines 503 and 506. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
6nzd
Structure name
cryo-em structure of the lysosomal folliculin complex (flcn-fnip2- raga-ragc-ragulator)
Structure deposition date
2019-02-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
46
Peptide accession
Q8NFG4
Residue number A
503
Residue number B
506
Peptide name
Folliculin

Ligandability

Cysteine 503 of Folliculin

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 506 of Folliculin

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 Folliculin between cysteines 82 and 85. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
6ulg
Structure name
cryo-em structure of the flcn-fnip2-rag-ragulator complex
Structure deposition date
2019-10-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
42
Peptide accession
Q8NFG4
Residue number A
82
Residue number B
85
Peptide name
Folliculin

Ligandability

Cysteine 82 of Folliculin

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 85 of Folliculin

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Folliculin between cysteines 8 and 21. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
6nzd
Structure name
cryo-em structure of the lysosomal folliculin complex (flcn-fnip2- raga-ragc-ragulator)
Structure deposition date
2019-02-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
nan
Peptide accession
Q8NFG4
Residue number A
8
Residue number B
21
Peptide name
Folliculin

Ligandability

Cysteine 8 of Folliculin

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 21 of Folliculin

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 Folliculin between cysteines 131 and 134. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
8dhb
Structure name
active flcn gap complex
Structure deposition date
2022-06-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
10
% buried
100
Peptide accession
Q8NFG4
Residue number A
131
Residue number B
134
Peptide name
Folliculin

Ligandability

Cysteine 131 of Folliculin

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 134 of Folliculin

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Folliculin between cysteines 21 and 125. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6nzd
Structure name
cryo-em structure of the lysosomal folliculin complex (flcn-fnip2- raga-ragc-ragulator)
Structure deposition date
2019-02-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
nan
Peptide accession
Q8NFG4
Residue number A
21
Residue number B
125
Peptide name
Folliculin

Ligandability

Cysteine 21 of Folliculin

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 125 of Folliculin

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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