LIM domain kinase 2
Intermolecular
Cysteine 365 and cysteine 549
Intramolecular
Cysteine 98 and cysteine 101
Cysteine 121 and cysteine 124
Cysteine 72 and cysteine 75
Cysteine 98 and cysteine 121
Cysteine 72 and cysteine 95
Cysteine 98 and cysteine 124
Cysteine 101 and cysteine 121
Cysteine 101 and cysteine 124
Cysteine 75 and cysteine 95
More...Cysteine 537 and cysteine 584
Cysteine 583 and cysteine 584
Cysteine 537 and cysteine 583
Cysteine 537 and cysteine 572
4tpt A 365 B 549
A redox-regulated disulphide may form between two units of LIM domain kinase 2 at cysteines 365 and 549.
Details
Redox score ?
85
PDB code
4tpt
Structure name
crystal structure of the human limk2 kinase domain in complex with a non-atp competitive inhibitor
Structure deposition date
2014-06-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide A name
LIM domain kinase 2
Peptide B name
LIM domain kinase 2
Peptide A accession
P53671
Peptide B accession
P53671
Peptide A residue number
365
Peptide B residue number
549
Ligandability
Cysteine 365 of LIM domain kinase 2
Cysteine 549 of LIM domain kinase 2
1x6a A 44 A 47
A redox-regulated disulphide may form within LIM domain kinase 2 between cysteines 98 and 101 (44 and 47 respectively in this structure).
Details
Redox score ?
84
PDB code
1x6a
Structure name
solution structures of the second lim domain of human lim-kinase 2 (limk2)
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
7
% buried
0
Peptide accession
P53671
Residue number A
98
Residue number B
101
Peptide name
LIM domain kinase 2
Ligandability
Cysteine 98 of LIM domain kinase 2
Cysteine 101 of LIM domain kinase 2
1x6a A 67 A 70
A redox-regulated disulphide may form within LIM domain kinase 2 between cysteines 121 and 124 (67 and 70 respectively in this structure).
Details
Redox score ?
83
PDB code
1x6a
Structure name
solution structures of the second lim domain of human lim-kinase 2 (limk2)
Structure deposition date
2005-05-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
0
Peptide accession
P53671
Residue number A
121
Residue number B
124
Peptide name
LIM domain kinase 2
Ligandability
Cysteine 121 of LIM domain kinase 2
Cysteine 124 of LIM domain kinase 2
1x6a A 18 A 21
A redox-regulated disulphide may form within LIM domain kinase 2 between cysteines 72 and 75 (18 and 21 respectively in this structure).
Details
Redox score ?
82
PDB code
1x6a
Structure name
solution structures of the second lim domain of human lim-kinase 2 (limk2)
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
7
% buried
3
Peptide accession
P53671
Residue number A
72
Residue number B
75
Peptide name
LIM domain kinase 2
Ligandability
Cysteine 72 of LIM domain kinase 2
Cysteine 75 of LIM domain kinase 2
1x6a A 44 A 67
A redox-regulated disulphide may form within LIM domain kinase 2 between cysteines 98 and 121 (44 and 67 respectively in this structure).
Details
Redox score ?
80
PDB code
1x6a
Structure name
solution structures of the second lim domain of human lim-kinase 2 (limk2)
Structure deposition date
2005-05-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
54
Minimum pKa ?
7
% buried
0
Peptide accession
P53671
Residue number A
98
Residue number B
121
Peptide name
LIM domain kinase 2
Ligandability
Cysteine 98 of LIM domain kinase 2
Cysteine 121 of LIM domain kinase 2
1x6a A 18 A 41
A redox-regulated disulphide may form within LIM domain kinase 2 between cysteines 72 and 95 (18 and 41 respectively in this structure).
Details
Redox score ?
78
PDB code
1x6a
Structure name
solution structures of the second lim domain of human lim-kinase 2 (limk2)
Structure deposition date
2005-05-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
52
Minimum pKa ?
7
% buried
4
Peptide accession
P53671
Residue number A
72
Residue number B
95
Peptide name
LIM domain kinase 2
Ligandability
Cysteine 72 of LIM domain kinase 2
Cysteine 95 of LIM domain kinase 2
1x6a A 44 A 70
A redox-regulated disulphide may form within LIM domain kinase 2 between cysteines 98 and 124 (44 and 70 respectively in this structure).
Details
Redox score ?
74
PDB code
1x6a
Structure name
solution structures of the second lim domain of human lim-kinase 2 (limk2)
Structure deposition date
2005-05-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
47
Minimum pKa ?
7
% buried
0
Peptide accession
P53671
Residue number A
98
Residue number B
124
Peptide name
LIM domain kinase 2
Ligandability
Cysteine 98 of LIM domain kinase 2
Cysteine 124 of LIM domain kinase 2
1x6a A 47 A 67
A redox-regulated disulphide may form within LIM domain kinase 2 between cysteines 101 and 121 (47 and 67 respectively in this structure).
Details
Redox score ?
71
PDB code
1x6a
Structure name
solution structures of the second lim domain of human lim-kinase 2 (limk2)
Structure deposition date
2005-05-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
0
Peptide accession
P53671
Residue number A
101
Residue number B
121
Peptide name
LIM domain kinase 2
Ligandability
Cysteine 101 of LIM domain kinase 2
Cysteine 121 of LIM domain kinase 2
1x6a A 47 A 70
A redox-regulated disulphide may form within LIM domain kinase 2 between cysteines 101 and 124 (47 and 70 respectively in this structure).
Details
Redox score ?
67
PDB code
1x6a
Structure name
solution structures of the second lim domain of human lim-kinase 2 (limk2)
Structure deposition date
2005-05-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
36
Minimum pKa ?
9
% buried
0
Peptide accession
P53671
Residue number A
101
Residue number B
124
Peptide name
LIM domain kinase 2
Ligandability
Cysteine 101 of LIM domain kinase 2
Cysteine 124 of LIM domain kinase 2
1x6a A 21 A 41
A redox-regulated disulphide may form within LIM domain kinase 2 between cysteines 75 and 95 (21 and 41 respectively in this structure).
Details
Redox score ?
64
PDB code
1x6a
Structure name
solution structures of the second lim domain of human lim-kinase 2 (limk2)
Structure deposition date
2005-05-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
0
Peptide accession
P53671
Residue number A
75
Residue number B
95
Peptide name
LIM domain kinase 2
Ligandability
Cysteine 75 of LIM domain kinase 2
Cysteine 95 of LIM domain kinase 2
7qhg B 537 B 584
A redox-regulated disulphide may form within LIM domain kinase 2 between cysteines 537 and 584. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
7qhg
Structure name
lim domain kinase 2 (limk2) in complex with th-470
Structure deposition date
2021-12-12
Thiol separation (Å)
5
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
100
Peptide accession
P53671
Residue number A
537
Residue number B
584
Peptide name
LIM domain kinase 2
Ligandability
Cysteine 537 of LIM domain kinase 2
Cysteine 584 of LIM domain kinase 2
4tpt A 583 A 584
A redox-regulated disulphide may form within LIM domain kinase 2 between cysteines 583 and 584. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
4tpt
Structure name
crystal structure of the human limk2 kinase domain in complex with a non-atp competitive inhibitor
Structure deposition date
2014-06-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
100
Peptide accession
P53671
Residue number A
583
Residue number B
584
Peptide name
LIM domain kinase 2
Ligandability
Cysteine 583 of LIM domain kinase 2
Cysteine 584 of LIM domain kinase 2
7qhg A 537 A 583
A redox-regulated disulphide may form within LIM domain kinase 2 between cysteines 537 and 583. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
7qhg
Structure name
lim domain kinase 2 (limk2) in complex with th-470
Structure deposition date
2021-12-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
13
% buried
100
Peptide accession
P53671
Residue number A
537
Residue number B
583
Peptide name
LIM domain kinase 2
Ligandability
Cysteine 537 of LIM domain kinase 2
Cysteine 583 of LIM domain kinase 2
7qhg A 537 A 572
A redox-regulated disulphide may form within LIM domain kinase 2 between cysteines 537 and 572. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
7qhg
Structure name
lim domain kinase 2 (limk2) in complex with th-470
Structure deposition date
2021-12-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
89
Peptide accession
P53671
Residue number A
537
Residue number B
572
Peptide name
LIM domain kinase 2
Ligandability
Cysteine 537 of LIM domain kinase 2
Cysteine 572 of LIM domain kinase 2
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