Beta-microseminoprotein
Intermolecular
Cysteine 22 and cysteine 22
Cysteine 22 and cysteine 70
Intramolecular
Cysteine 57 and cysteine 93
Cysteine 84 and cysteine 107
Cysteine 38 and cysteine 62
Cysteine 60 and cysteine 69
Cysteine 60 and cysteine 62
Cysteine 62 and cysteine 69
Cysteine 69 and cysteine 70
Cysteine 60 and cysteine 70
More...Cysteine 22 and cysteine 69
Cysteine 38 and cysteine 60
Cysteine 22 and cysteine 60
Cysteine 57 and cysteine 70
Cysteine 38 and cysteine 69
3ix0 A 2 B 2
A redox-regulated disulphide may form between two units of Beta-microseminoprotein at cysteines 22 and 22 (2 and 2 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
3ix0
Structure name
crystal structure of human seminal plasma protein psp94
Structure deposition date
2009-09-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide A name
Beta-microseminoprotein
Peptide B name
Beta-microseminoprotein
Peptide A accession
P08118
Peptide B accession
P08118
Peptide A residue number
22
Peptide B residue number
22
Ligandability
3ix0 A 2 B 50
A redox-regulated disulphide may form between two units of Beta-microseminoprotein at cysteines 22 and 70 (2 and 50 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
3ix0
Structure name
crystal structure of human seminal plasma protein psp94
Structure deposition date
2009-09-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide A name
Beta-microseminoprotein
Peptide B name
Beta-microseminoprotein
Peptide A accession
P08118
Peptide B accession
P08118
Peptide A residue number
22
Peptide B residue number
70
Ligandability
Cysteine 22 of Beta-microseminoprotein
Cysteine 70 of Beta-microseminoprotein
3ix0 A 37 A 73
A redox-regulated disulphide may form within Beta-microseminoprotein between cysteines 57 and 93 (37 and 73 respectively in this structure).
Details
Redox score ?
86
PDB code
3ix0
Structure name
crystal structure of human seminal plasma protein psp94
Structure deposition date
2009-09-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08118
Residue number A
57
Residue number B
93
Peptide name
Beta-microseminoprotein
Ligandability
Cysteine 57 of Beta-microseminoprotein
Cysteine 93 of Beta-microseminoprotein
3ix0 B 64 B 87
A redox-regulated disulphide may form within Beta-microseminoprotein between cysteines 84 and 107 (64 and 87 respectively in this structure).
Details
Redox score ?
84
PDB code
3ix0
Structure name
crystal structure of human seminal plasma protein psp94
Structure deposition date
2009-09-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08118
Residue number A
84
Residue number B
107
Peptide name
Beta-microseminoprotein
Ligandability
Cysteine 84 of Beta-microseminoprotein
Cysteine 107 of Beta-microseminoprotein
3ix0 C 18 C 42
A redox-regulated disulphide may form within Beta-microseminoprotein between cysteines 38 and 62 (18 and 42 respectively in this structure).
Details
Redox score ?
84
PDB code
3ix0
Structure name
crystal structure of human seminal plasma protein psp94
Structure deposition date
2009-09-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08118
Residue number A
38
Residue number B
62
Peptide name
Beta-microseminoprotein
Ligandability
Cysteine 38 of Beta-microseminoprotein
Cysteine 62 of Beta-microseminoprotein
3ix0 B 40 B 49
A redox-regulated disulphide may form within Beta-microseminoprotein between cysteines 60 and 69 (40 and 49 respectively in this structure).
Details
Redox score ?
83
PDB code
3ix0
Structure name
crystal structure of human seminal plasma protein psp94
Structure deposition date
2009-09-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08118
Residue number A
60
Residue number B
69
Peptide name
Beta-microseminoprotein
Ligandability
Cysteine 60 of Beta-microseminoprotein
Cysteine 69 of Beta-microseminoprotein
3ix0 D 40 D 42
A redox-regulated disulphide may form within Beta-microseminoprotein between cysteines 60 and 62 (40 and 42 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
3ix0
Structure name
crystal structure of human seminal plasma protein psp94
Structure deposition date
2009-09-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08118
Residue number A
60
Residue number B
62
Peptide name
Beta-microseminoprotein
Ligandability
Cysteine 60 of Beta-microseminoprotein
Cysteine 62 of Beta-microseminoprotein
3ix0 D 42 D 49
A redox-regulated disulphide may form within Beta-microseminoprotein between cysteines 62 and 69 (42 and 49 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
3ix0
Structure name
crystal structure of human seminal plasma protein psp94
Structure deposition date
2009-09-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08118
Residue number A
62
Residue number B
69
Peptide name
Beta-microseminoprotein
Ligandability
Cysteine 62 of Beta-microseminoprotein
Cysteine 69 of Beta-microseminoprotein
3ix0 C 49 C 50
A redox-regulated disulphide may form within Beta-microseminoprotein between cysteines 69 and 70 (49 and 50 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
3ix0
Structure name
crystal structure of human seminal plasma protein psp94
Structure deposition date
2009-09-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08118
Residue number A
69
Residue number B
70
Peptide name
Beta-microseminoprotein
Ligandability
Cysteine 69 of Beta-microseminoprotein
Cysteine 70 of Beta-microseminoprotein
3ix0 B 40 B 50
A redox-regulated disulphide may form within Beta-microseminoprotein between cysteines 60 and 70 (40 and 50 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
3ix0
Structure name
crystal structure of human seminal plasma protein psp94
Structure deposition date
2009-09-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08118
Residue number A
60
Residue number B
70
Peptide name
Beta-microseminoprotein
Ligandability
Cysteine 60 of Beta-microseminoprotein
Cysteine 70 of Beta-microseminoprotein
3ix0 C 2 C 49
A redox-regulated disulphide may form within Beta-microseminoprotein between cysteines 22 and 69 (2 and 49 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
3ix0
Structure name
crystal structure of human seminal plasma protein psp94
Structure deposition date
2009-09-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08118
Residue number A
22
Residue number B
69
Peptide name
Beta-microseminoprotein
Ligandability
Cysteine 22 of Beta-microseminoprotein
Cysteine 69 of Beta-microseminoprotein
3ix0 D 18 D 40
A redox-regulated disulphide may form within Beta-microseminoprotein between cysteines 38 and 60 (18 and 40 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
3ix0
Structure name
crystal structure of human seminal plasma protein psp94
Structure deposition date
2009-09-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08118
Residue number A
38
Residue number B
60
Peptide name
Beta-microseminoprotein
Ligandability
Cysteine 38 of Beta-microseminoprotein
Cysteine 60 of Beta-microseminoprotein
3ix0 D 2 D 40
A redox-regulated disulphide may form within Beta-microseminoprotein between cysteines 22 and 60 (2 and 40 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
3ix0
Structure name
crystal structure of human seminal plasma protein psp94
Structure deposition date
2009-09-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08118
Residue number A
22
Residue number B
60
Peptide name
Beta-microseminoprotein
Ligandability
Cysteine 22 of Beta-microseminoprotein
Cysteine 60 of Beta-microseminoprotein
2iz3 A 37 A 50
A redox-regulated disulphide may form within Beta-microseminoprotein between cysteines 57 and 70 (37 and 50 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
2iz3
Structure name
solution structure of human beta-microseminoprotein
Structure deposition date
2006-07-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08118
Residue number A
57
Residue number B
70
Peptide name
Beta-microseminoprotein
Ligandability
Cysteine 57 of Beta-microseminoprotein
Cysteine 70 of Beta-microseminoprotein
3ix0 D 18 D 49
A redox-regulated disulphide may form within Beta-microseminoprotein between cysteines 38 and 69 (18 and 49 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
3ix0
Structure name
crystal structure of human seminal plasma protein psp94
Structure deposition date
2009-09-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08118
Residue number A
38
Residue number B
69
Peptide name
Beta-microseminoprotein
Ligandability
Cysteine 38 of Beta-microseminoprotein
Cysteine 69 of Beta-microseminoprotein
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