ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Sperm-egg fusion protein Juno

Intramolecular
Cysteine 79 and cysteine 172
Cysteine 47 and cysteine 95
Cysteine 86 and cysteine 143
Cysteine 149 and cysteine 166
Cysteine 136 and cysteine 186
Cysteine 132 and cysteine 206
Cysteine 56 and cysteine 99
Cysteine 27 and cysteine 55
Cysteine 79 and cysteine 166
Cysteine 166 and cysteine 172
More...
Cysteine 47 and cysteine 99
Cysteine 79 and cysteine 160
Cysteine 79 and cysteine 149
Cysteine 149 and cysteine 172
Cysteine 47 and cysteine 56
Cysteine 95 and cysteine 99
Cysteine 56 and cysteine 95
Cysteine 55 and cysteine 56
Cysteine 55 and cysteine 99
Cysteine 132 and cysteine 136
Cysteine 27 and cysteine 56
Cysteine 136 and cysteine 206
Cysteine 143 and cysteine 186
Cysteine 27 and cysteine 99
Cysteine 132 and cysteine 186
A redox-regulated disulphide may form within Sperm-egg fusion protein Juno between cysteines 79 and 172.

Details

Redox score ?
86
PDB code
5f4q
Structure name
crystal structure of the human egg surface protein juno
Structure deposition date
2015-12-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
79
Residue number B
172
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 79 of Sperm-egg fusion protein Juno

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 172 of Sperm-egg fusion protein Juno

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 Juno between cysteines 47 and 95.

Details

Redox score ?
84
PDB code
5f4q
Structure name
crystal structure of the human egg surface protein juno
Structure deposition date
2015-12-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
47
Residue number B
95
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 47 of Sperm-egg fusion protein Juno

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 Sperm-egg fusion protein Juno

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 Juno between cysteines 86 and 143.

Details

Redox score ?
83
PDB code
5jkb
Structure name
crystal structure of human juno (crystal form 2)
Structure deposition date
2016-04-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
86
Residue number B
143
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 86 of Sperm-egg fusion protein Juno

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 143 of Sperm-egg fusion protein Juno

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 Juno between cysteines 149 and 166.

Details

Redox score ?
83
PDB code
5f4q
Structure name
crystal structure of the human egg surface protein juno
Structure deposition date
2015-12-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
149
Residue number B
166
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 149 of Sperm-egg fusion protein Juno

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 166 of Sperm-egg fusion protein Juno

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 Juno between cysteines 136 and 186.

Details

Redox score ?
81
PDB code
5f4q
Structure name
crystal structure of the human egg surface protein juno
Structure deposition date
2015-12-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
136
Residue number B
186
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 136 of Sperm-egg fusion protein Juno

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 186 of Sperm-egg fusion protein Juno

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 Juno between cysteines 132 and 206.

Details

Redox score ?
80
PDB code
5f4q
Structure name
crystal structure of the human egg surface protein juno
Structure deposition date
2015-12-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
132
Residue number B
206
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 132 of Sperm-egg fusion protein Juno

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 206 of Sperm-egg fusion protein Juno

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 Juno between cysteines 56 and 99.

Details

Redox score ?
80
PDB code
5f4e
Structure name
crystal structure of the human sperm izumo1 and egg juno complex
Structure deposition date
2015-12-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
92
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
56
Residue number B
99
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 56 of Sperm-egg fusion protein Juno

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 99 of Sperm-egg fusion protein Juno

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 Juno between cysteines 27 and 55.

Details

Redox score ?
79
PDB code
5f4q
Structure name
crystal structure of the human egg surface protein juno
Structure deposition date
2015-12-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
27
Residue number B
55
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 27 of Sperm-egg fusion protein Juno

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 55 of Sperm-egg fusion protein Juno

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 Juno between cysteines 79 and 166.

Details

Redox score ?
74
PDB code
5jkb
Structure name
crystal structure of human juno (crystal form 2)
Structure deposition date
2016-04-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
79
Residue number B
166
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 79 of Sperm-egg fusion protein Juno

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 166 of Sperm-egg fusion protein Juno

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 Juno between cysteines 166 and 172.

Details

Redox score ?
73
PDB code
5jkb
Structure name
crystal structure of human juno (crystal form 2)
Structure deposition date
2016-04-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
166
Residue number B
172
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 166 of Sperm-egg fusion protein Juno

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 172 of Sperm-egg fusion protein Juno

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 Juno between cysteines 47 and 99.

Details

Redox score ?
71
PDB code
5jkc
Structure name
crystal structure of human izumo1-juno complex (crystal form 1)
Structure deposition date
2016-04-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
91
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
47
Residue number B
99
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 47 of Sperm-egg fusion protein Juno

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 99 of Sperm-egg fusion protein Juno

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 Juno between cysteines 79 and 160.

Details

Redox score ?
69
PDB code
5jyj
Structure name
crystal structure of mouse juno
Structure deposition date
2016-05-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9EQF4
Residue number A
79
Residue number B
160
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 79 of Sperm-egg fusion protein Juno

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 160 of Sperm-egg fusion protein Juno

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 Juno between cysteines 79 and 149.

Details

Redox score ?
67
PDB code
5f4e
Structure name
crystal structure of the human sperm izumo1 and egg juno complex
Structure deposition date
2015-12-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
79
Residue number B
149
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 79 of Sperm-egg fusion protein Juno

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 149 of Sperm-egg fusion protein Juno

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 Juno between cysteines 149 and 172.

Details

Redox score ?
65
PDB code
5f4q
Structure name
crystal structure of the human egg surface protein juno
Structure deposition date
2015-12-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
149
Residue number B
172
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 149 of Sperm-egg fusion protein Juno

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 172 of Sperm-egg fusion protein Juno

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 Juno between cysteines 47 and 56.

Details

Redox score ?
64
PDB code
5f4q
Structure name
crystal structure of the human egg surface protein juno
Structure deposition date
2015-12-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
47
Residue number B
56
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 47 of Sperm-egg fusion protein Juno

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 56 of Sperm-egg fusion protein Juno

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 Juno between cysteines 95 and 99.

Details

Redox score ?
64
PDB code
5f4q
Structure name
crystal structure of the human egg surface protein juno
Structure deposition date
2015-12-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
95
Residue number B
99
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 95 of Sperm-egg fusion protein Juno

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 99 of Sperm-egg fusion protein Juno

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 Juno between cysteines 56 and 95. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
5jke
Structure name
crystal structure of human izumo1-juno complex (crystal form 3)
Structure deposition date
2016-04-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
56
Residue number B
95
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 56 of Sperm-egg fusion protein Juno

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 Sperm-egg fusion protein Juno

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 Juno between cysteines 55 and 56. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
5jke
Structure name
crystal structure of human izumo1-juno complex (crystal form 3)
Structure deposition date
2016-04-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
55
Residue number B
56
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 55 of Sperm-egg fusion protein Juno

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 56 of Sperm-egg fusion protein Juno

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 Juno between cysteines 55 and 99. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
5f4e
Structure name
crystal structure of the human sperm izumo1 and egg juno complex
Structure deposition date
2015-12-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
55
Residue number B
99
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 55 of Sperm-egg fusion protein Juno

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 99 of Sperm-egg fusion protein Juno

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 Juno between cysteines 132 and 136. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
5jke
Structure name
crystal structure of human izumo1-juno complex (crystal form 3)
Structure deposition date
2016-04-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
132
Residue number B
136
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 132 of Sperm-egg fusion protein Juno

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 136 of Sperm-egg fusion protein Juno

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 Juno between cysteines 27 and 56. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
5f4q
Structure name
crystal structure of the human egg surface protein juno
Structure deposition date
2015-12-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
27
Residue number B
56
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 27 of Sperm-egg fusion protein Juno

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 56 of Sperm-egg fusion protein Juno

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 Juno between cysteines 136 and 206. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5f4q
Structure name
crystal structure of the human egg surface protein juno
Structure deposition date
2015-12-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
136
Residue number B
206
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 136 of Sperm-egg fusion protein Juno

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 206 of Sperm-egg fusion protein Juno

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 Juno between cysteines 143 and 186. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5f4q
Structure name
crystal structure of the human egg surface protein juno
Structure deposition date
2015-12-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
143
Residue number B
186
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 143 of Sperm-egg fusion protein Juno

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 186 of Sperm-egg fusion protein Juno

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 Juno between cysteines 27 and 99. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
5f4e
Structure name
crystal structure of the human sperm izumo1 and egg juno complex
Structure deposition date
2015-12-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
27
Residue number B
99
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 27 of Sperm-egg fusion protein Juno

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 99 of Sperm-egg fusion protein Juno

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 Juno between cysteines 132 and 186. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
5f4q
Structure name
crystal structure of the human egg surface protein juno
Structure deposition date
2015-12-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6ND01
Residue number A
132
Residue number B
186
Peptide name
Sperm-egg fusion protein Juno

Ligandability

Cysteine 132 of Sperm-egg fusion protein Juno

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 186 of Sperm-egg fusion protein Juno

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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