Cyclin-dependent kinase inhibitor 3
Intramolecular
Cysteine 119 and cysteine 153
Cysteine 119 and cysteine 120
Cysteine 51 and cysteine 79 L
Cysteine 46 and cysteine 70
Cysteine 46 and cysteine 79
1fq1 A 119 A 153
A redox-regulated disulphide may form within Cyclin-dependent kinase inhibitor 3 between cysteines 119 and 153.
Details
Redox score ?
69
PDB code
1fq1
Structure name
crystal structure of kinase associated phosphatase (kap) in complex with phospho-cdk2
Structure deposition date
2000-09-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
7
% buried
90
Peptide accession
Q16667
Residue number A
119
Residue number B
153
Peptide name
Cyclin-dependent kinase inhibitor 3
Ligandability
Cysteine 119 of Cyclin-dependent kinase inhibitor 3
Cysteine 153 of Cyclin-dependent kinase inhibitor 3
1fpz E 119 E 120
A redox-regulated disulphide may form within Cyclin-dependent kinase inhibitor 3 between cysteines 119 and 120. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
1fpz
Structure name
crystal structure analysis of kinase associated phosphatase (kap) with a substitution of the catalytic site cysteine (cys140) to a serine
Structure deposition date
2000-09-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
42
Peptide accession
Q16667
Residue number A
119
Residue number B
120
Peptide name
Cyclin-dependent kinase inhibitor 3
Ligandability
Cysteine 119 of Cyclin-dependent kinase inhibitor 3
Cysteine 120 of Cyclin-dependent kinase inhibitor 3
1fpz D 51 D 79
A redox-regulated disulphide may form within Cyclin-dependent kinase inhibitor 3 between cysteines 51 and 79. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
1fpz
Structure name
crystal structure analysis of kinase associated phosphatase (kap) with a substitution of the catalytic site cysteine (cys140) to a serine
Structure deposition date
2000-09-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
54
Peptide accession
Q16667
Residue number A
51
Residue number B
79
Peptide name
Cyclin-dependent kinase inhibitor 3
Ligandability
Cysteine 51 of Cyclin-dependent kinase inhibitor 3
Cysteine 79 of Cyclin-dependent kinase inhibitor 3
1fpz C 46 C 70
A redox-regulated disulphide may form within Cyclin-dependent kinase inhibitor 3 between cysteines 46 and 70. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
1fpz
Structure name
crystal structure analysis of kinase associated phosphatase (kap) with a substitution of the catalytic site cysteine (cys140) to a serine
Structure deposition date
2000-09-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
58
Peptide accession
Q16667
Residue number A
46
Residue number B
70
Peptide name
Cyclin-dependent kinase inhibitor 3
Ligandability
Cysteine 46 of Cyclin-dependent kinase inhibitor 3
Cysteine 70 of Cyclin-dependent kinase inhibitor 3
1fpz B 46 B 79
A redox-regulated disulphide may form within Cyclin-dependent kinase inhibitor 3 between cysteines 46 and 79. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
1fpz
Structure name
crystal structure analysis of kinase associated phosphatase (kap) with a substitution of the catalytic site cysteine (cys140) to a serine
Structure deposition date
2000-09-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
90
Peptide accession
Q16667
Residue number A
46
Residue number B
79
Peptide name
Cyclin-dependent kinase inhibitor 3
Ligandability
Cysteine 46 of Cyclin-dependent kinase inhibitor 3
Cysteine 79 of Cyclin-dependent kinase inhibitor 3
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