Acrosin
Intermolecular
Cysteine 152 and cysteine 22
Cysteine 160 and cysteine 26
Intramolecular
Cysteine 175 and cysteine 244
Cysteine 234 and cysteine 264
Cysteine 207 and cysteine 223
Cysteine 71 and cysteine 87
1fiz A 114 L 5
A redox-regulated disulphide may form between two units of Acrosin at cysteines 152 and 22 (114 and 5 respectively in this structure).
Details
Redox score ?
87
PDB code
1fiz
Structure name
three dimensional structure of beta-acrosin from boar spermatozoa
Structure deposition date
2000-08-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide A name
Acrosin
Peptide B name
Acrosin
Peptide A accession
P08001
Peptide B accession
P08001
Peptide A residue number
152
Peptide B residue number
22
Ligandability
Cysteine 152 of Acrosin
Cysteine 22 of Acrosin
1fiz A 122 L 9
A redox-regulated disulphide may form between two units of Acrosin at cysteines 160 and 26 (122 and 9 respectively in this structure).
Details
Redox score ?
80
PDB code
1fiz
Structure name
three dimensional structure of beta-acrosin from boar spermatozoa
Structure deposition date
2000-08-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide A name
Acrosin
Peptide B name
Acrosin
Peptide A accession
P08001
Peptide B accession
P08001
Peptide A residue number
160
Peptide B residue number
26
Ligandability
Cysteine 160 of Acrosin
Cysteine 26 of Acrosin
1fiw A 136 A 201
A redox-regulated disulphide may form within Acrosin between cysteines 175 and 244 (136 and 201 respectively in this structure).
Details
Redox score ?
82
PDB code
1fiw
Structure name
three-dimensional structure of beta-acrosin from ram spermatozoa
Structure deposition date
2000-08-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9GL10
Residue number A
175
Residue number B
244
Peptide name
Acrosin
Ligandability
Cysteine 175 of Acrosin
Cysteine 244 of Acrosin
1fiw A 191 A 220
A redox-regulated disulphide may form within Acrosin between cysteines 234 and 264 (191 and 220 respectively in this structure).
Details
Redox score ?
80
PDB code
1fiw
Structure name
three-dimensional structure of beta-acrosin from ram spermatozoa
Structure deposition date
2000-08-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9GL10
Residue number A
234
Residue number B
264
Peptide name
Acrosin
Ligandability
Cysteine 234 of Acrosin
Cysteine 264 of Acrosin
1fiz A 168 A 182
A redox-regulated disulphide may form within Acrosin between cysteines 207 and 223 (168 and 182 respectively in this structure).
Details
Redox score ?
79
PDB code
1fiz
Structure name
three dimensional structure of beta-acrosin from boar spermatozoa
Structure deposition date
2000-08-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08001
Residue number A
207
Residue number B
223
Peptide name
Acrosin
Ligandability
Cysteine 207 of Acrosin
Cysteine 223 of Acrosin
1fiw A 42 A 58
A redox-regulated disulphide may form within Acrosin between cysteines 71 and 87 (42 and 58 respectively in this structure).
Details
Redox score ?
79
PDB code
1fiw
Structure name
three-dimensional structure of beta-acrosin from ram spermatozoa
Structure deposition date
2000-08-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9GL10
Residue number A
71
Residue number B
87
Peptide name
Acrosin
Ligandability
Cysteine 71 of Acrosin
Cysteine 87 of Acrosin
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