ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Hyccin

Intramolecular
Cysteine 57 and cysteine 100
Cysteine 207 and cysteine 211
Cysteine 204 and cysteine 207
Cysteine 57 and cysteine 85
Cysteine 211 and cysteine 213
A redox-regulated disulphide may form within Hyccin between cysteines 57 and 100.

Details

Redox score ?
66
PDB code
5dse
Structure name
crystal structure of the ttc7b/hyccin complex
Structure deposition date
2015-09-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
30
Peptide accession
Q9BYI3
Residue number A
57
Residue number B
100
Peptide name
Hyccin

Ligandability

Cysteine 57 of Hyccin

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 100 of Hyccin

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 Hyccin between cysteines 207 and 211. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
5dse
Structure name
crystal structure of the ttc7b/hyccin complex
Structure deposition date
2015-09-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
100
Peptide accession
Q9BYI3
Residue number A
207
Residue number B
211
Peptide name
Hyccin

Ligandability

Cysteine 207 of Hyccin

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 211 of Hyccin

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 Hyccin between cysteines 204 and 207. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
5dse
Structure name
crystal structure of the ttc7b/hyccin complex
Structure deposition date
2015-09-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
96
Peptide accession
Q9BYI3
Residue number A
204
Residue number B
207
Peptide name
Hyccin

Ligandability

Cysteine 204 of Hyccin

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 Hyccin

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 Hyccin between cysteines 57 and 85. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5dse
Structure name
crystal structure of the ttc7b/hyccin complex
Structure deposition date
2015-09-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
74
Peptide accession
Q9BYI3
Residue number A
57
Residue number B
85
Peptide name
Hyccin

Ligandability

Cysteine 57 of Hyccin

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 Hyccin

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 Hyccin between cysteines 211 and 213. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
6bq1
Structure name
human pi4kiiia lipid kinase complex
Structure deposition date
2017-11-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
80
Peptide accession
Q9BYI3
Residue number A
211
Residue number B
213
Peptide name
Hyccin

Ligandability

Cysteine 211 of Hyccin

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 213 of Hyccin

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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