Carboxypeptidase B
Intramolecular
Cysteine 245 and cysteine 268
Cysteine 259 and cysteine 273
Cysteine 173 and cysteine 186
Cysteine 173 and cysteine 398
Cysteine 186 and cysteine 398
1kwm A 138 A 161
A redox-regulated disulphide may form within Carboxypeptidase B between cysteines 245 and 268 (138 and 161 respectively in this structure).
Details
Redox score ?
84
PDB code
1kwm
Structure name
human procarboxypeptidase b: three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (tafi)
Structure deposition date
2002-01-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15086
Residue number A
245
Residue number B
268
Peptide name
Carboxypeptidase B
Ligandability
Cysteine 245 of Carboxypeptidase B
Cysteine 268 of Carboxypeptidase B
1kwm A 152 A 166
A redox-regulated disulphide may form within Carboxypeptidase B between cysteines 259 and 273 (152 and 166 respectively in this structure).
Details
Redox score ?
83
PDB code
1kwm
Structure name
human procarboxypeptidase b: three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (tafi)
Structure deposition date
2002-01-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15086
Residue number A
259
Residue number B
273
Peptide name
Carboxypeptidase B
Ligandability
Cysteine 259 of Carboxypeptidase B
Cysteine 273 of Carboxypeptidase B
1kwm A 66 A 79
A redox-regulated disulphide may form within Carboxypeptidase B between cysteines 173 and 186 (66 and 79 respectively in this structure).
Details
Redox score ?
77
PDB code
1kwm
Structure name
human procarboxypeptidase b: three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (tafi)
Structure deposition date
2002-01-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
92
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15086
Residue number A
173
Residue number B
186
Peptide name
Carboxypeptidase B
Ligandability
Cysteine 173 of Carboxypeptidase B
Cysteine 186 of Carboxypeptidase B
1kwm A 66 A 290
A redox-regulated disulphide may form within Carboxypeptidase B between cysteines 173 and 398 (66 and 290 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
1kwm
Structure name
human procarboxypeptidase b: three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (tafi)
Structure deposition date
2002-01-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
13
% buried
nan
Peptide accession
P15086
Residue number A
173
Residue number B
398
Peptide name
Carboxypeptidase B
Ligandability
Cysteine 173 of Carboxypeptidase B
Cysteine 398 of Carboxypeptidase B
1kwm A 79 A 290
A redox-regulated disulphide may form within Carboxypeptidase B between cysteines 186 and 398 (79 and 290 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
1kwm
Structure name
human procarboxypeptidase b: three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (tafi)
Structure deposition date
2002-01-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
13
% buried
nan
Peptide accession
P15086
Residue number A
186
Residue number B
398
Peptide name
Carboxypeptidase B
Ligandability
Cysteine 186 of Carboxypeptidase B
Cysteine 398 of Carboxypeptidase B
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