ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Sperm-egg fusion protein TMEM95

Intramolecular
Cysteine 17 and cysteine 118
Cysteine 109 and cysteine 128
Cysteine 35 and cysteine 45
Cysteine 105 and cysteine 134
Cysteine 20 and cysteine 121
Cysteine 20 and cysteine 118
Cysteine 17 and cysteine 20
Cysteine 109 and cysteine 134
Cysteine 105 and cysteine 109
Cysteine 128 and cysteine 134
More...
Cysteine 118 and cysteine 121
Cysteine 17 and cysteine 121
Cysteine 105 and cysteine 128
A redox-regulated disulphide may form within Sperm-egg fusion protein TMEM95 between cysteines 17 and 118.

Details

Redox score ?
90
PDB code
7ux0
Structure name
human sperm tmem95 ectodomain
Structure deposition date
2022-05-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3KNT9
Residue number A
17
Residue number B
118
Peptide name
Sperm-egg fusion protein TMEM95

Ligandability

Cysteine 17 of Sperm-egg fusion protein TMEM95

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 118 of Sperm-egg fusion protein TMEM95

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 Sperm-egg fusion protein TMEM95 between cysteines 109 and 128.

Details

Redox score ?
90
PDB code
7ux0
Structure name
human sperm tmem95 ectodomain
Structure deposition date
2022-05-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3KNT9
Residue number A
109
Residue number B
128
Peptide name
Sperm-egg fusion protein TMEM95

Ligandability

Cysteine 109 of Sperm-egg fusion protein TMEM95

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 128 of Sperm-egg fusion protein TMEM95

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 Sperm-egg fusion protein TMEM95 between cysteines 35 and 45.

Details

Redox score ?
88
PDB code
7ux0
Structure name
human sperm tmem95 ectodomain
Structure deposition date
2022-05-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3KNT9
Residue number A
35
Residue number B
45
Peptide name
Sperm-egg fusion protein TMEM95

Ligandability

Cysteine 35 of Sperm-egg fusion protein TMEM95

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 45 of Sperm-egg fusion protein TMEM95

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 Sperm-egg fusion protein TMEM95 between cysteines 105 and 134.

Details

Redox score ?
87
PDB code
7ux0
Structure name
human sperm tmem95 ectodomain
Structure deposition date
2022-05-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3KNT9
Residue number A
105
Residue number B
134
Peptide name
Sperm-egg fusion protein TMEM95

Ligandability

Cysteine 105 of Sperm-egg fusion protein TMEM95

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 134 of Sperm-egg fusion protein TMEM95

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 Sperm-egg fusion protein TMEM95 between cysteines 20 and 121.

Details

Redox score ?
85
PDB code
7ux0
Structure name
human sperm tmem95 ectodomain
Structure deposition date
2022-05-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3KNT9
Residue number A
20
Residue number B
121
Peptide name
Sperm-egg fusion protein TMEM95

Ligandability

Cysteine 20 of Sperm-egg fusion protein TMEM95

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 121 of Sperm-egg fusion protein TMEM95

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 Sperm-egg fusion protein TMEM95 between cysteines 20 and 118.

Details

Redox score ?
60
PDB code
7ux0
Structure name
human sperm tmem95 ectodomain
Structure deposition date
2022-05-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3KNT9
Residue number A
20
Residue number B
118
Peptide name
Sperm-egg fusion protein TMEM95

Ligandability

Cysteine 20 of Sperm-egg fusion protein TMEM95

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 118 of Sperm-egg fusion protein TMEM95

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 Sperm-egg fusion protein TMEM95 between cysteines 17 and 20. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
7ux0
Structure name
human sperm tmem95 ectodomain
Structure deposition date
2022-05-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3KNT9
Residue number A
17
Residue number B
20
Peptide name
Sperm-egg fusion protein TMEM95

Ligandability

Cysteine 17 of Sperm-egg fusion protein TMEM95

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 20 of Sperm-egg fusion protein TMEM95

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 Sperm-egg fusion protein TMEM95 between cysteines 109 and 134. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
7ux0
Structure name
human sperm tmem95 ectodomain
Structure deposition date
2022-05-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3KNT9
Residue number A
109
Residue number B
134
Peptide name
Sperm-egg fusion protein TMEM95

Ligandability

Cysteine 109 of Sperm-egg fusion protein TMEM95

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 134 of Sperm-egg fusion protein TMEM95

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 Sperm-egg fusion protein TMEM95 between cysteines 105 and 109. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
7ux0
Structure name
human sperm tmem95 ectodomain
Structure deposition date
2022-05-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3KNT9
Residue number A
105
Residue number B
109
Peptide name
Sperm-egg fusion protein TMEM95

Ligandability

Cysteine 105 of Sperm-egg fusion protein TMEM95

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 109 of Sperm-egg fusion protein TMEM95

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 Sperm-egg fusion protein TMEM95 between cysteines 128 and 134. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
7ux0
Structure name
human sperm tmem95 ectodomain
Structure deposition date
2022-05-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3KNT9
Residue number A
128
Residue number B
134
Peptide name
Sperm-egg fusion protein TMEM95

Ligandability

Cysteine 128 of Sperm-egg fusion protein TMEM95

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 134 of Sperm-egg fusion protein TMEM95

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 Sperm-egg fusion protein TMEM95 between cysteines 118 and 121. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
7ux0
Structure name
human sperm tmem95 ectodomain
Structure deposition date
2022-05-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3KNT9
Residue number A
118
Residue number B
121
Peptide name
Sperm-egg fusion protein TMEM95

Ligandability

Cysteine 118 of Sperm-egg fusion protein TMEM95

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 121 of Sperm-egg fusion protein TMEM95

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 Sperm-egg fusion protein TMEM95 between cysteines 17 and 121. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
7ux0
Structure name
human sperm tmem95 ectodomain
Structure deposition date
2022-05-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3KNT9
Residue number A
17
Residue number B
121
Peptide name
Sperm-egg fusion protein TMEM95

Ligandability

Cysteine 17 of Sperm-egg fusion protein TMEM95

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 121 of Sperm-egg fusion protein TMEM95

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 Sperm-egg fusion protein TMEM95 between cysteines 105 and 128. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
7ux0
Structure name
human sperm tmem95 ectodomain
Structure deposition date
2022-05-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q3KNT9
Residue number A
105
Residue number B
128
Peptide name
Sperm-egg fusion protein TMEM95

Ligandability

Cysteine 105 of Sperm-egg fusion protein TMEM95

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 128 of Sperm-egg fusion protein TMEM95

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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