Tyrosine-protein kinase
Intramolecular
Cysteine 506 and cysteine 633
Cysteine 481 and cysteine 527
Cysteine 502 and cysteine 506
Cysteine 502 and cysteine 633
Cysteine 502 and cysteine 527
6mny A 506 A 633
A redox-regulated disulphide may form within Tyrosine-protein kinase between cysteines 506 and 633. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
6mny
Structure name
crystal structure of mouse btk kinase domain in complex with compound 9a
Structure deposition date
2018-10-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
96
Peptide accession
Q7TMU1
Residue number A
506
Residue number B
633
Peptide name
Tyrosine-protein kinase
Ligandability
Cysteine 506 of Tyrosine-protein kinase
Cysteine 633 of Tyrosine-protein kinase
6mny A 481 A 527
A redox-regulated disulphide may form within Tyrosine-protein kinase between cysteines 481 and 527. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
6mny
Structure name
crystal structure of mouse btk kinase domain in complex with compound 9a
Structure deposition date
2018-10-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
88
Peptide accession
Q7TMU1
Residue number A
481
Residue number B
527
Peptide name
Tyrosine-protein kinase
Ligandability
Cysteine 481 of Tyrosine-protein kinase
Cysteine 527 of Tyrosine-protein kinase
6mny B 502 B 506
A redox-regulated disulphide may form within Tyrosine-protein kinase between cysteines 502 and 506. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
6mny
Structure name
crystal structure of mouse btk kinase domain in complex with compound 9a
Structure deposition date
2018-10-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
89
Minimum pKa ?
13
% buried
96
Peptide accession
Q7TMU1
Residue number A
502
Residue number B
506
Peptide name
Tyrosine-protein kinase
Ligandability
Cysteine 502 of Tyrosine-protein kinase
Cysteine 506 of Tyrosine-protein kinase
6mny B 502 B 633
A redox-regulated disulphide may form within Tyrosine-protein kinase between cysteines 502 and 633. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
6mny
Structure name
crystal structure of mouse btk kinase domain in complex with compound 9a
Structure deposition date
2018-10-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
100
Peptide accession
Q7TMU1
Residue number A
502
Residue number B
633
Peptide name
Tyrosine-protein kinase
Ligandability
Cysteine 502 of Tyrosine-protein kinase
Cysteine 633 of Tyrosine-protein kinase
6mny B 502 B 527
A redox-regulated disulphide may form within Tyrosine-protein kinase between cysteines 502 and 527. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
24
PDB code
6mny
Structure name
crystal structure of mouse btk kinase domain in complex with compound 9a
Structure deposition date
2018-10-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
89
Minimum pKa ?
13
% buried
100
Peptide accession
Q7TMU1
Residue number A
502
Residue number B
527
Peptide name
Tyrosine-protein kinase
Ligandability
Cysteine 502 of Tyrosine-protein kinase
Cysteine 527 of Tyrosine-protein kinase
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