Inactive tyrosine-protein kinase PRAG1
Intramolecular
Cysteine 970 and cysteine 1385
Cysteine 996 and cysteine 1010
Cysteine 1000 and cysteine 1010
Cysteine 1000 and cysteine 1001
Cysteine 1346 and cysteine 1347
Cysteine 996 and cysteine 1000
Cysteine 1303 and cysteine 1310
Cysteine 999 and cysteine 1010
Cysteine 1026 and cysteine 1087
Cysteine 1013 and cysteine 1051
5ve6 A 970 A 1385
A redox-regulated disulphide may form within Inactive tyrosine-protein kinase PRAG1 between cysteines 970 and 1385.
Details
Redox score ?
63
PDB code
5ve6
Structure name
crystal structure of sugen kinase 223
Structure deposition date
2017-04-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
59
Peptide accession
Q86YV5
Residue number A
970
Residue number B
1385
Peptide name
Inactive tyrosine-protein kinase PRAG1
Ligandability
Cysteine 970 of Inactive tyrosine-protein kinase PRAG1
Cysteine 1385 of Inactive tyrosine-protein kinase PRAG1
5ve6 A 996 A 1010
A redox-regulated disulphide may form within Inactive tyrosine-protein kinase PRAG1 between cysteines 996 and 1010. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
5ve6
Structure name
crystal structure of sugen kinase 223
Structure deposition date
2017-04-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
10
Peptide accession
Q86YV5
Residue number A
996
Residue number B
1010
Peptide name
Inactive tyrosine-protein kinase PRAG1
Ligandability
Cysteine 996 of Inactive tyrosine-protein kinase PRAG1
Cysteine 1010 of Inactive tyrosine-protein kinase PRAG1
5ve6 A 1000 A 1010
A redox-regulated disulphide may form within Inactive tyrosine-protein kinase PRAG1 between cysteines 1000 and 1010. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
5ve6
Structure name
crystal structure of sugen kinase 223
Structure deposition date
2017-04-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
37
Peptide accession
Q86YV5
Residue number A
1000
Residue number B
1010
Peptide name
Inactive tyrosine-protein kinase PRAG1
Ligandability
Cysteine 1000 of Inactive tyrosine-protein kinase PRAG1
Cysteine 1010 of Inactive tyrosine-protein kinase PRAG1
5ve6 A 1000 A 1001
A redox-regulated disulphide may form within Inactive tyrosine-protein kinase PRAG1 between cysteines 1000 and 1001. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
5ve6
Structure name
crystal structure of sugen kinase 223
Structure deposition date
2017-04-03
Thiol separation (Å)
6
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
60
Peptide accession
Q86YV5
Residue number A
1000
Residue number B
1001
Peptide name
Inactive tyrosine-protein kinase PRAG1
Ligandability
Cysteine 1000 of Inactive tyrosine-protein kinase PRAG1
Cysteine 1001 of Inactive tyrosine-protein kinase PRAG1
6ewx A 1346 A 1347
A redox-regulated disulphide may form within Inactive tyrosine-protein kinase PRAG1 between cysteines 1346 and 1347. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
6ewx
Structure name
structure of pragmin pseudo-kinase reveals a dimerization mechanism to regulate protein tyrosine phosphorylation and nuclear transcription
Structure deposition date
2017-11-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
91
Peptide accession
D3ZMK9
Residue number A
1346
Residue number B
1347
Peptide name
Inactive tyrosine-protein kinase PRAG1
Ligandability
Cysteine 1346 of Inactive tyrosine-protein kinase PRAG1
Cysteine 1347 of Inactive tyrosine-protein kinase PRAG1
5ve6 A 996 A 1000
A redox-regulated disulphide may form within Inactive tyrosine-protein kinase PRAG1 between cysteines 996 and 1000. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
5ve6
Structure name
crystal structure of sugen kinase 223
Structure deposition date
2017-04-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
48
Minimum pKa ?
8
% buried
28
Peptide accession
Q86YV5
Residue number A
996
Residue number B
1000
Peptide name
Inactive tyrosine-protein kinase PRAG1
Ligandability
Cysteine 996 of Inactive tyrosine-protein kinase PRAG1
Cysteine 1000 of Inactive tyrosine-protein kinase PRAG1
6ewx B 1303 B 1310
A redox-regulated disulphide may form within Inactive tyrosine-protein kinase PRAG1 between cysteines 1303 and 1310. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
6ewx
Structure name
structure of pragmin pseudo-kinase reveals a dimerization mechanism to regulate protein tyrosine phosphorylation and nuclear transcription
Structure deposition date
2017-11-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
3
Peptide accession
D3ZMK9
Residue number A
1303
Residue number B
1310
Peptide name
Inactive tyrosine-protein kinase PRAG1
Ligandability
Cysteine 1303 of Inactive tyrosine-protein kinase PRAG1
Cysteine 1310 of Inactive tyrosine-protein kinase PRAG1
6ewx B 999 B 1010
A redox-regulated disulphide may form within Inactive tyrosine-protein kinase PRAG1 between cysteines 999 and 1010. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
6ewx
Structure name
structure of pragmin pseudo-kinase reveals a dimerization mechanism to regulate protein tyrosine phosphorylation and nuclear transcription
Structure deposition date
2017-11-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
28
Peptide accession
D3ZMK9
Residue number A
999
Residue number B
1010
Peptide name
Inactive tyrosine-protein kinase PRAG1
Ligandability
Cysteine 999 of Inactive tyrosine-protein kinase PRAG1
Cysteine 1010 of Inactive tyrosine-protein kinase PRAG1
5ve6 A 1026 A 1087
A redox-regulated disulphide may form within Inactive tyrosine-protein kinase PRAG1 between cysteines 1026 and 1087. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
5ve6
Structure name
crystal structure of sugen kinase 223
Structure deposition date
2017-04-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
28
Peptide accession
Q86YV5
Residue number A
1026
Residue number B
1087
Peptide name
Inactive tyrosine-protein kinase PRAG1
Ligandability
Cysteine 1026 of Inactive tyrosine-protein kinase PRAG1
Cysteine 1087 of Inactive tyrosine-protein kinase PRAG1
5ve6 A 1013 A 1051
A redox-regulated disulphide may form within Inactive tyrosine-protein kinase PRAG1 between cysteines 1013 and 1051. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
5ve6
Structure name
crystal structure of sugen kinase 223
Structure deposition date
2017-04-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
25
Peptide accession
Q86YV5
Residue number A
1013
Residue number B
1051
Peptide name
Inactive tyrosine-protein kinase PRAG1
Ligandability
Cysteine 1013 of Inactive tyrosine-protein kinase PRAG1
Cysteine 1051 of Inactive tyrosine-protein kinase PRAG1
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