Mitochondrial Rho GTPase 2
Intermolecular
Cysteine 470 and cysteine 470
Intramolecular
Cysteine 419 and cysteine 490
Cysteine 419 and cysteine 486
Cysteine 486 and cysteine 519
Cysteine 470 and cysteine 486
Cysteine 504 and cysteine 543 L
Cysteine 519 and cysteine 543 L
Cysteine 419 and cysteine 470
Cysteine 486 and cysteine 490
Cysteine 490 and cysteine 504
More...Cysteine 504 and cysteine 519
Cysteine 419 and cysteine 519
Cysteine 490 and cysteine 519
5kut B 470 C 470
A redox-regulated disulphide may form between two units of Mitochondrial Rho GTPase 2 at cysteines 470 and 470. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5kut
Structure name
hmiro2 c-terminal gtpase domain, gdp-bound
Structure deposition date
2016-07-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
100
Peptide A name
Mitochondrial Rho GTPase 2
Peptide B name
Mitochondrial Rho GTPase 2
Peptide A accession
Q8IXI1
Peptide B accession
Q8IXI1
Peptide A residue number
470
Peptide B residue number
470
Ligandability
5kut B 419 B 490
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 2 between cysteines 419 and 490. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
5kut
Structure name
hmiro2 c-terminal gtpase domain, gdp-bound
Structure deposition date
2016-07-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
92
Minimum pKa ?
13
% buried
100
Peptide accession
Q8IXI1
Residue number A
419
Residue number B
490
Peptide name
Mitochondrial Rho GTPase 2
Ligandability
Cysteine 419 of Mitochondrial Rho GTPase 2
Cysteine 490 of Mitochondrial Rho GTPase 2
5kut B 419 B 486
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 2 between cysteines 419 and 486. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
5kut
Structure name
hmiro2 c-terminal gtpase domain, gdp-bound
Structure deposition date
2016-07-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
11
% buried
91
Peptide accession
Q8IXI1
Residue number A
419
Residue number B
486
Peptide name
Mitochondrial Rho GTPase 2
Ligandability
Cysteine 419 of Mitochondrial Rho GTPase 2
Cysteine 486 of Mitochondrial Rho GTPase 2
5kut C 486 C 519
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 2 between cysteines 486 and 519. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5kut
Structure name
hmiro2 c-terminal gtpase domain, gdp-bound
Structure deposition date
2016-07-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
92
Peptide accession
Q8IXI1
Residue number A
486
Residue number B
519
Peptide name
Mitochondrial Rho GTPase 2
Ligandability
Cysteine 486 of Mitochondrial Rho GTPase 2
Cysteine 519 of Mitochondrial Rho GTPase 2
5kut A 470 A 486
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 2 between cysteines 470 and 486. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
5kut
Structure name
hmiro2 c-terminal gtpase domain, gdp-bound
Structure deposition date
2016-07-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
55
Peptide accession
Q8IXI1
Residue number A
470
Residue number B
486
Peptide name
Mitochondrial Rho GTPase 2
Ligandability
Cysteine 470 of Mitochondrial Rho GTPase 2
Cysteine 486 of Mitochondrial Rho GTPase 2
5kut A 504 A 543
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 2 between cysteines 504 and 543. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
5kut
Structure name
hmiro2 c-terminal gtpase domain, gdp-bound
Structure deposition date
2016-07-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
78
Peptide accession
Q8IXI1
Residue number A
504
Residue number B
543
Peptide name
Mitochondrial Rho GTPase 2
Ligandability
Cysteine 504 of Mitochondrial Rho GTPase 2
Cysteine 543 of Mitochondrial Rho GTPase 2
5kut A 519 A 543
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 2 between cysteines 519 and 543. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
5kut
Structure name
hmiro2 c-terminal gtpase domain, gdp-bound
Structure deposition date
2016-07-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
72
Peptide accession
Q8IXI1
Residue number A
519
Residue number B
543
Peptide name
Mitochondrial Rho GTPase 2
Ligandability
Cysteine 519 of Mitochondrial Rho GTPase 2
Cysteine 543 of Mitochondrial Rho GTPase 2
5kut B 419 B 470
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 2 between cysteines 419 and 470. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
5kut
Structure name
hmiro2 c-terminal gtpase domain, gdp-bound
Structure deposition date
2016-07-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
100
Peptide accession
Q8IXI1
Residue number A
419
Residue number B
470
Peptide name
Mitochondrial Rho GTPase 2
Ligandability
Cysteine 419 of Mitochondrial Rho GTPase 2
Cysteine 470 of Mitochondrial Rho GTPase 2
5kut A 486 A 490
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 2 between cysteines 486 and 490. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
5kut
Structure name
hmiro2 c-terminal gtpase domain, gdp-bound
Structure deposition date
2016-07-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
11
% buried
84
Peptide accession
Q8IXI1
Residue number A
486
Residue number B
490
Peptide name
Mitochondrial Rho GTPase 2
Ligandability
Cysteine 486 of Mitochondrial Rho GTPase 2
Cysteine 490 of Mitochondrial Rho GTPase 2
5kut B 490 B 504
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 2 between cysteines 490 and 504. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
5kut
Structure name
hmiro2 c-terminal gtpase domain, gdp-bound
Structure deposition date
2016-07-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
92
Minimum pKa ?
13
% buried
100
Peptide accession
Q8IXI1
Residue number A
490
Residue number B
504
Peptide name
Mitochondrial Rho GTPase 2
Ligandability
Cysteine 490 of Mitochondrial Rho GTPase 2
Cysteine 504 of Mitochondrial Rho GTPase 2
5kut A 504 A 519
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 2 between cysteines 504 and 519. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
5kut
Structure name
hmiro2 c-terminal gtpase domain, gdp-bound
Structure deposition date
2016-07-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
92
Minimum pKa ?
13
% buried
95
Peptide accession
Q8IXI1
Residue number A
504
Residue number B
519
Peptide name
Mitochondrial Rho GTPase 2
Ligandability
Cysteine 504 of Mitochondrial Rho GTPase 2
Cysteine 519 of Mitochondrial Rho GTPase 2
5kut C 419 C 519
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 2 between cysteines 419 and 519. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
5kut
Structure name
hmiro2 c-terminal gtpase domain, gdp-bound
Structure deposition date
2016-07-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
13
% buried
92
Peptide accession
Q8IXI1
Residue number A
419
Residue number B
519
Peptide name
Mitochondrial Rho GTPase 2
Ligandability
Cysteine 419 of Mitochondrial Rho GTPase 2
Cysteine 519 of Mitochondrial Rho GTPase 2
5kut A 490 A 519
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 2 between cysteines 490 and 519. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
23
PDB code
5kut
Structure name
hmiro2 c-terminal gtpase domain, gdp-bound
Structure deposition date
2016-07-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
97
Minimum pKa ?
13
% buried
95
Peptide accession
Q8IXI1
Residue number A
490
Residue number B
519
Peptide name
Mitochondrial Rho GTPase 2
Ligandability
Cysteine 490 of Mitochondrial Rho GTPase 2
Cysteine 519 of Mitochondrial Rho GTPase 2
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