Tyrosine-protein kinase BTK
Intermolecular
Cysteine 481 and cysteine 315 of Baculoviral IAP repeat-containing protein 2 L
Intramolecular
Cysteine 154 and cysteine 155
Cysteine 155 and cysteine 165
Cysteine 154 and cysteine 165
Cysteine 145 and cysteine 154
Cysteine 145 and cysteine 165
Cysteine 145 and cysteine 155
Cysteine 506 and cysteine 633
Cysteine 502 and cysteine 506
Cysteine 481 and cysteine 527 L
More...Cysteine 502 and cysteine 633
Cysteine 502 and cysteine 527
6w7o B 481 D 315
A redox-regulated disulphide may form between cysteine 481 of Tyrosine-protein kinase BTK and cysteine 315 of Baculoviral IAP repeat-containing protein 2. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
6w7o
Structure name
ternary complex structure - btk ciap compound 17
Structure deposition date
2020-03-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
100
Peptide A name
Tyrosine-protein kinase BTK
Peptide B name
Baculoviral IAP repeat-containing protein 2
Peptide A accession
Q06187
Peptide B accession
Q13490
Peptide A residue number
481
Peptide B residue number
315
Ligandability
Cysteine 481 of Tyrosine-protein kinase BTK
Cysteine 315 of Baculoviral IAP repeat-containing protein 2
1b55 B 154 B 155
A redox-regulated disulphide may form within Tyrosine-protein kinase BTK between cysteines 154 and 155.
Details
Redox score ?
85
PDB code
1b55
Structure name
ph domain from bruton's tyrosine kinase in complex with inositol 1,3, 4,5-tetrakisphosphate
Structure deposition date
1999-01-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
48
Minimum pKa ?
7
% buried
19
Peptide accession
Q06187
Residue number A
154
Residue number B
155
Peptide name
Tyrosine-protein kinase BTK
Ligandability
Cysteine 154 of Tyrosine-protein kinase BTK
Cysteine 155 of Tyrosine-protein kinase BTK
1b55 B 155 B 165
A redox-regulated disulphide may form within Tyrosine-protein kinase BTK between cysteines 155 and 165.
Details
Redox score ?
83
PDB code
1b55
Structure name
ph domain from bruton's tyrosine kinase in complex with inositol 1,3, 4,5-tetrakisphosphate
Structure deposition date
1999-01-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
44
Minimum pKa ?
7
% buried
4
Peptide accession
Q06187
Residue number A
155
Residue number B
165
Peptide name
Tyrosine-protein kinase BTK
Ligandability
Cysteine 155 of Tyrosine-protein kinase BTK
Cysteine 165 of Tyrosine-protein kinase BTK
6tt2 B 154 B 165
A redox-regulated disulphide may form within Tyrosine-protein kinase BTK between cysteines 154 and 165.
Details
Redox score ?
80
PDB code
6tt2
Structure name
the ph domain of bruton's tyrosine kinase mutant r28c
Structure deposition date
2019-12-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
9
% buried
22
Peptide accession
Q06187
Residue number A
154
Residue number B
165
Peptide name
Tyrosine-protein kinase BTK
Ligandability
Cysteine 154 of Tyrosine-protein kinase BTK
Cysteine 165 of Tyrosine-protein kinase BTK
1bwn B 145 B 154
A redox-regulated disulphide may form within Tyrosine-protein kinase BTK between cysteines 145 and 154.
Details
Redox score ?
71
PDB code
1bwn
Structure name
ph domain and btk motif from bruton's tyrosine kinase mutant e41k in complex with ins(1,3,4,5)p4
Structure deposition date
1998-09-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
30
Peptide accession
Q06187
Residue number A
145
Residue number B
154
Peptide name
Tyrosine-protein kinase BTK
Ligandability
Cysteine 145 of Tyrosine-protein kinase BTK
Cysteine 154 of Tyrosine-protein kinase BTK
6tse A 145 A 165
A redox-regulated disulphide may form within Tyrosine-protein kinase BTK between cysteines 145 and 165. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
6tse
Structure name
crystal structure of 1-methylindoline-2,3-dione covalently bound to the ph domain of bruton's tyrosine kinase mutant r28c
Structure deposition date
2019-12-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
50
Minimum pKa ?
10
% buried
19
Peptide accession
Q06187
Residue number A
145
Residue number B
165
Peptide name
Tyrosine-protein kinase BTK
Ligandability
Cysteine 145 of Tyrosine-protein kinase BTK
Cysteine 165 of Tyrosine-protein kinase BTK
6tt2 A 145 A 155
A redox-regulated disulphide may form within Tyrosine-protein kinase BTK between cysteines 145 and 155. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
6tt2
Structure name
the ph domain of bruton's tyrosine kinase mutant r28c
Structure deposition date
2019-12-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
13
Peptide accession
Q06187
Residue number A
145
Residue number B
155
Peptide name
Tyrosine-protein kinase BTK
Ligandability
Cysteine 145 of Tyrosine-protein kinase BTK
Cysteine 155 of Tyrosine-protein kinase BTK
4xi2 A 506 A 633
A redox-regulated disulphide may form within Tyrosine-protein kinase BTK 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 ?
47
PDB code
4xi2
Structure name
crystal structure of an auto-inhibited form of bruton's tryrosine kinase
Structure deposition date
2015-01-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35991
Residue number A
506
Residue number B
633
Peptide name
Tyrosine-protein kinase BTK
Ligandability
Cysteine 506 of Tyrosine-protein kinase BTK
Cysteine 633 of Tyrosine-protein kinase BTK
4xi2 A 502 A 506
A redox-regulated disulphide may form within Tyrosine-protein kinase BTK 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 ?
41
PDB code
4xi2
Structure name
crystal structure of an auto-inhibited form of bruton's tryrosine kinase
Structure deposition date
2015-01-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35991
Residue number A
502
Residue number B
506
Peptide name
Tyrosine-protein kinase BTK
Ligandability
Cysteine 502 of Tyrosine-protein kinase BTK
Cysteine 506 of Tyrosine-protein kinase BTK
1k2p A 481 A 527
A redox-regulated disulphide may form within Tyrosine-protein kinase BTK 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 ?
41
PDB code
1k2p
Structure name
crystal structure of bruton's tyrosine kinase domain
Structure deposition date
2001-09-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
8
% buried
100
Peptide accession
Q06187
Residue number A
481
Residue number B
527
Peptide name
Tyrosine-protein kinase BTK
Ligandability
Cysteine 481 of Tyrosine-protein kinase BTK
Cysteine 527 of Tyrosine-protein kinase BTK
4xi2 A 502 A 633
A redox-regulated disulphide may form within Tyrosine-protein kinase BTK 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 ?
36
PDB code
4xi2
Structure name
crystal structure of an auto-inhibited form of bruton's tryrosine kinase
Structure deposition date
2015-01-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35991
Residue number A
502
Residue number B
633
Peptide name
Tyrosine-protein kinase BTK
Ligandability
Cysteine 502 of Tyrosine-protein kinase BTK
Cysteine 633 of Tyrosine-protein kinase BTK
4xi2 A 502 A 527
A redox-regulated disulphide may form within Tyrosine-protein kinase BTK 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 ?
36
PDB code
4xi2
Structure name
crystal structure of an auto-inhibited form of bruton's tryrosine kinase
Structure deposition date
2015-01-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35991
Residue number A
502
Residue number B
527
Peptide name
Tyrosine-protein kinase BTK
Ligandability
Cysteine 502 of Tyrosine-protein kinase BTK
Cysteine 527 of Tyrosine-protein kinase BTK
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