Cyclin-dependent kinase-like 1
Intramolecular
Cysteine 118 and cysteine 123
Cysteine 268 and cysteine 279
Cysteine 84 and cysteine 144
Cysteine 118 and cysteine 279
Cysteine 191 and cysteine 268
4agu A 117 A 122
A redox-regulated disulphide may form within Cyclin-dependent kinase-like 1 between cysteines 118 and 123 (117 and 122 respectively in this structure).
Details
Redox score ?
70
PDB code
4agu
Structure name
crystal structure of the human cdkl1 kinase domain
Structure deposition date
2012-01-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
8
% buried
80
Peptide accession
Q00532
Residue number A
118
Residue number B
123
Peptide name
Cyclin-dependent kinase-like 1
Ligandability
Cysteine 118 of Cyclin-dependent kinase-like 1
Cysteine 123 of Cyclin-dependent kinase-like 1
4agu B 267 B 278
A redox-regulated disulphide may form within Cyclin-dependent kinase-like 1 between cysteines 268 and 279 (267 and 278 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
4agu
Structure name
crystal structure of the human cdkl1 kinase domain
Structure deposition date
2012-01-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
100
Peptide accession
Q00532
Residue number A
268
Residue number B
279
Peptide name
Cyclin-dependent kinase-like 1
Ligandability
Cysteine 268 of Cyclin-dependent kinase-like 1
Cysteine 279 of Cyclin-dependent kinase-like 1
4agu A 83 A 143
A redox-regulated disulphide may form within Cyclin-dependent kinase-like 1 between cysteines 84 and 144 (83 and 143 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
4agu
Structure name
crystal structure of the human cdkl1 kinase domain
Structure deposition date
2012-01-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
13
% buried
93
Peptide accession
Q00532
Residue number A
84
Residue number B
144
Peptide name
Cyclin-dependent kinase-like 1
Ligandability
Cysteine 84 of Cyclin-dependent kinase-like 1
Cysteine 144 of Cyclin-dependent kinase-like 1
4agu C 117 C 278
A redox-regulated disulphide may form within Cyclin-dependent kinase-like 1 between cysteines 118 and 279 (117 and 278 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
4agu
Structure name
crystal structure of the human cdkl1 kinase domain
Structure deposition date
2012-01-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
13
% buried
94
Peptide accession
Q00532
Residue number A
118
Residue number B
279
Peptide name
Cyclin-dependent kinase-like 1
Ligandability
Cysteine 118 of Cyclin-dependent kinase-like 1
Cysteine 279 of Cyclin-dependent kinase-like 1
4agu C 190 C 267
A redox-regulated disulphide may form within Cyclin-dependent kinase-like 1 between cysteines 191 and 268 (190 and 267 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
4agu
Structure name
crystal structure of the human cdkl1 kinase domain
Structure deposition date
2012-01-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
100
Peptide accession
Q00532
Residue number A
191
Residue number B
268
Peptide name
Cyclin-dependent kinase-like 1
Ligandability
Cysteine 191 of Cyclin-dependent kinase-like 1
Cysteine 268 of Cyclin-dependent kinase-like 1
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