Rho-associated protein kinase 2
Intramolecular
Cysteine 1296 and cysteine 1315
Cysteine 1293 and cysteine 1315
Cysteine 1274 and cysteine 1277
Cysteine 1293 and cysteine 1296
Cysteine 1274 and cysteine 1300
Cysteine 1277 and cysteine 1300
Cysteine 247 and cysteine 275
Cysteine 1293 and cysteine 1300
Cysteine 1296 and cysteine 1300
Cysteine 314 and cysteine 330
Cysteine 236 and cysteine 275
2row A 60 A 79
A redox-regulated disulphide may form within Rho-associated protein kinase 2 between cysteines 1296 and 1315 (60 and 79 respectively in this structure).
Details
Redox score ?
86
PDB code
2row
Structure name
the c1 domain of rock ii
Structure deposition date
2008-04-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
6
% buried
12
Peptide accession
Q62868
Residue number A
1296
Residue number B
1315
Peptide name
Rho-associated protein kinase 2
Ligandability
Cysteine 1296 of Rho-associated protein kinase 2
Cysteine 1315 of Rho-associated protein kinase 2
2row A 57 A 79
A redox-regulated disulphide may form within Rho-associated protein kinase 2 between cysteines 1293 and 1315 (57 and 79 respectively in this structure).
Details
Redox score ?
86
PDB code
2row
Structure name
the c1 domain of rock ii
Structure deposition date
2008-04-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
6
% buried
18
Peptide accession
Q62868
Residue number A
1293
Residue number B
1315
Peptide name
Rho-associated protein kinase 2
Ligandability
Cysteine 1293 of Rho-associated protein kinase 2
Cysteine 1315 of Rho-associated protein kinase 2
2row A 38 A 41
A redox-regulated disulphide may form within Rho-associated protein kinase 2 between cysteines 1274 and 1277 (38 and 41 respectively in this structure).
Details
Redox score ?
81
PDB code
2row
Structure name
the c1 domain of rock ii
Structure deposition date
2008-04-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
8
% buried
18
Peptide accession
Q62868
Residue number A
1274
Residue number B
1277
Peptide name
Rho-associated protein kinase 2
Ligandability
Cysteine 1274 of Rho-associated protein kinase 2
Cysteine 1277 of Rho-associated protein kinase 2
2row A 57 A 60
A redox-regulated disulphide may form within Rho-associated protein kinase 2 between cysteines 1293 and 1296 (57 and 60 respectively in this structure).
Details
Redox score ?
79
PDB code
2row
Structure name
the c1 domain of rock ii
Structure deposition date
2008-04-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
27
Peptide accession
Q62868
Residue number A
1293
Residue number B
1296
Peptide name
Rho-associated protein kinase 2
Ligandability
Cysteine 1293 of Rho-associated protein kinase 2
Cysteine 1296 of Rho-associated protein kinase 2
2row A 38 A 64
A redox-regulated disulphide may form within Rho-associated protein kinase 2 between cysteines 1274 and 1300 (38 and 64 respectively in this structure).
Details
Redox score ?
70
PDB code
2row
Structure name
the c1 domain of rock ii
Structure deposition date
2008-04-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
47
Peptide accession
Q62868
Residue number A
1274
Residue number B
1300
Peptide name
Rho-associated protein kinase 2
Ligandability
Cysteine 1274 of Rho-associated protein kinase 2
Cysteine 1300 of Rho-associated protein kinase 2
2row A 41 A 64
A redox-regulated disulphide may form within Rho-associated protein kinase 2 between cysteines 1277 and 1300 (41 and 64 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
2row
Structure name
the c1 domain of rock ii
Structure deposition date
2008-04-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
8
% buried
30
Peptide accession
Q62868
Residue number A
1277
Residue number B
1300
Peptide name
Rho-associated protein kinase 2
Ligandability
Cysteine 1277 of Rho-associated protein kinase 2
Cysteine 1300 of Rho-associated protein kinase 2
7jov H 247 H 275
A redox-regulated disulphide may form within Rho-associated protein kinase 2 between cysteines 247 and 275. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
7jov
Structure name
crystal structure of rho-associated protein kinase 2 (rock2) in complex with a phenylpyrazole amide inhibitor
Structure deposition date
2020-08-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
60
Peptide accession
O75116
Residue number A
247
Residue number B
275
Peptide name
Rho-associated protein kinase 2
Ligandability
Cysteine 247 of Rho-associated protein kinase 2
Cysteine 275 of Rho-associated protein kinase 2
2row A 57 A 64
A redox-regulated disulphide may form within Rho-associated protein kinase 2 between cysteines 1293 and 1300 (57 and 64 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
2row
Structure name
the c1 domain of rock ii
Structure deposition date
2008-04-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
9
% buried
46
Peptide accession
Q62868
Residue number A
1293
Residue number B
1300
Peptide name
Rho-associated protein kinase 2
Ligandability
Cysteine 1293 of Rho-associated protein kinase 2
Cysteine 1300 of Rho-associated protein kinase 2
2row A 60 A 64
A redox-regulated disulphide may form within Rho-associated protein kinase 2 between cysteines 1296 and 1300 (60 and 64 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
2row
Structure name
the c1 domain of rock ii
Structure deposition date
2008-04-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
40
Peptide accession
Q62868
Residue number A
1296
Residue number B
1300
Peptide name
Rho-associated protein kinase 2
Ligandability
Cysteine 1296 of Rho-associated protein kinase 2
Cysteine 1300 of Rho-associated protein kinase 2
2h9v A 314 A 330
A redox-regulated disulphide may form within Rho-associated protein kinase 2 between cysteines 314 and 330. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
2h9v
Structure name
structural basis for induced-fit binding of rho-kinase to the inhibitor y27632
Structure deposition date
2006-06-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
28
Peptide accession
Q28021
Residue number A
314
Residue number B
330
Peptide name
Rho-associated protein kinase 2
Ligandability
Cysteine 314 of Rho-associated protein kinase 2
Cysteine 330 of Rho-associated protein kinase 2
6p5m D 236 D 275
A redox-regulated disulphide may form within Rho-associated protein kinase 2 between cysteines 236 and 275. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
6p5m
Structure name
discovery of a novel, highly potent, and selective thieno[3,2- d]pyrimidinone-based cdc7 inhibitor with a quinuclidine moiety (tak- 931) as an orally active investigational anti-tumor agent
Structure deposition date
2019-05-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
O75116
Residue number A
236
Residue number B
275
Peptide name
Rho-associated protein kinase 2
Ligandability
Cysteine 236 of Rho-associated protein kinase 2
Cysteine 275 of Rho-associated protein kinase 2
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