Mitochondrial Rho GTPase 1
Intramolecular
Cysteine 421 and cysteine 493
Cysteine 421 and cysteine 489
Cysteine 429 and cysteine 507
Cysteine 429 and cysteine 493
Cysteine 507 and cysteine 546
Cysteine 489 and cysteine 522
Cysteine 507 and cysteine 522
Cysteine 489 and cysteine 493
Cysteine 493 and cysteine 522
Cysteine 522 and cysteine 546
More...Cysteine 493 and cysteine 507
Cysteine 421 and cysteine 522
Cysteine 79 and cysteine 147
5ksy A 421 A 493
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 1 between cysteines 421 and 493.
Details
Redox score ?
61
PDB code
5ksy
Structure name
hmiro1 c-domain gdp complex p41212 crystal form
Structure deposition date
2016-07-10
Thiol separation (Å)
5
Half-sphere exposure sum ?
91
Minimum pKa ?
9
% buried
100
Peptide accession
Q8IXI2
Residue number A
421
Residue number B
493
Peptide name
Mitochondrial Rho GTPase 1
Ligandability
Cysteine 421 of Mitochondrial Rho GTPase 1
Cysteine 493 of Mitochondrial Rho GTPase 1
5ksp A 421 A 489
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 1 between cysteines 421 and 489. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
5ksp
Structure name
hmiro1 c-domain gdp complex c2221 crystal form
Structure deposition date
2016-07-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
86
Peptide accession
Q8IXI2
Residue number A
421
Residue number B
489
Peptide name
Mitochondrial Rho GTPase 1
Ligandability
Cysteine 421 of Mitochondrial Rho GTPase 1
Cysteine 489 of Mitochondrial Rho GTPase 1
5ksz A 429 A 507
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 1 between cysteines 429 and 507. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5ksz
Structure name
hmiro ef hand and cgtpase domains in the gmppcp-bound state
Structure deposition date
2016-07-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
13
% buried
96
Peptide accession
Q8IXI2
Residue number A
429
Residue number B
507
Peptide name
Mitochondrial Rho GTPase 1
Ligandability
Cysteine 429 of Mitochondrial Rho GTPase 1
Cysteine 507 of Mitochondrial Rho GTPase 1
5kty A 429 A 493
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 1 between cysteines 429 and 493. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
5kty
Structure name
hmiro ef hand and cgtpase domains, gdp and ca2+ bound state
Structure deposition date
2016-07-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
9
% buried
100
Peptide accession
Q8IXI2
Residue number A
429
Residue number B
493
Peptide name
Mitochondrial Rho GTPase 1
Ligandability
Cysteine 429 of Mitochondrial Rho GTPase 1
Cysteine 493 of Mitochondrial Rho GTPase 1
5ku1 A 507 A 546
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 1 between cysteines 507 and 546. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
5ku1
Structure name
hmiro1 ef hand and cgtpase domains in the gdp-bound state
Structure deposition date
2016-07-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
76
Peptide accession
Q8IXI2
Residue number A
507
Residue number B
546
Peptide name
Mitochondrial Rho GTPase 1
Ligandability
Cysteine 507 of Mitochondrial Rho GTPase 1
Cysteine 546 of Mitochondrial Rho GTPase 1
5kso A 489 A 522
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 1 between cysteines 489 and 522. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
5kso
Structure name
hmiro1 c-domain gdp-pi complex p3121 crystal form
Structure deposition date
2016-07-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
82
Peptide accession
Q8IXI2
Residue number A
489
Residue number B
522
Peptide name
Mitochondrial Rho GTPase 1
Ligandability
Cysteine 489 of Mitochondrial Rho GTPase 1
Cysteine 522 of Mitochondrial Rho GTPase 1
5kty A 507 A 522
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 1 between cysteines 507 and 522. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
5kty
Structure name
hmiro ef hand and cgtpase domains, gdp and ca2+ bound state
Structure deposition date
2016-07-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
100
Peptide accession
Q8IXI2
Residue number A
507
Residue number B
522
Peptide name
Mitochondrial Rho GTPase 1
Ligandability
Cysteine 507 of Mitochondrial Rho GTPase 1
Cysteine 522 of Mitochondrial Rho GTPase 1
5kty A 489 A 493
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 1 between cysteines 489 and 493. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
5kty
Structure name
hmiro ef hand and cgtpase domains, gdp and ca2+ bound state
Structure deposition date
2016-07-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
9
% buried
100
Peptide accession
Q8IXI2
Residue number A
489
Residue number B
493
Peptide name
Mitochondrial Rho GTPase 1
Ligandability
Cysteine 489 of Mitochondrial Rho GTPase 1
Cysteine 493 of Mitochondrial Rho GTPase 1
5ku1 A 493 A 522
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 1 between cysteines 493 and 522. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
5ku1
Structure name
hmiro1 ef hand and cgtpase domains in the gdp-bound state
Structure deposition date
2016-07-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
93
Minimum pKa ?
9
% buried
96
Peptide accession
Q8IXI2
Residue number A
493
Residue number B
522
Peptide name
Mitochondrial Rho GTPase 1
Ligandability
Cysteine 493 of Mitochondrial Rho GTPase 1
Cysteine 522 of Mitochondrial Rho GTPase 1
5ku1 A 522 A 546
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 1 between cysteines 522 and 546. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
5ku1
Structure name
hmiro1 ef hand and cgtpase domains in the gdp-bound state
Structure deposition date
2016-07-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
72
Peptide accession
Q8IXI2
Residue number A
522
Residue number B
546
Peptide name
Mitochondrial Rho GTPase 1
Ligandability
Cysteine 522 of Mitochondrial Rho GTPase 1
Cysteine 546 of Mitochondrial Rho GTPase 1
5ksp A 493 A 507
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 1 between cysteines 493 and 507. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
5ksp
Structure name
hmiro1 c-domain gdp complex c2221 crystal form
Structure deposition date
2016-07-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
91
Minimum pKa ?
12
% buried
100
Peptide accession
Q8IXI2
Residue number A
493
Residue number B
507
Peptide name
Mitochondrial Rho GTPase 1
Ligandability
Cysteine 493 of Mitochondrial Rho GTPase 1
Cysteine 507 of Mitochondrial Rho GTPase 1
5ksy A 421 A 522
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 1 between cysteines 421 and 522. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
5ksy
Structure name
hmiro1 c-domain gdp complex p41212 crystal form
Structure deposition date
2016-07-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
13
% buried
97
Peptide accession
Q8IXI2
Residue number A
421
Residue number B
522
Peptide name
Mitochondrial Rho GTPase 1
Ligandability
Cysteine 421 of Mitochondrial Rho GTPase 1
Cysteine 522 of Mitochondrial Rho GTPase 1
6d71 A 79 A 147
A redox-regulated disulphide may form within Mitochondrial Rho GTPase 1 between cysteines 79 and 147. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
6d71
Structure name
crystal structure of the human miro1 n-terminal gtpase bound to gtp
Structure deposition date
2018-04-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
91
Minimum pKa ?
12
% buried
100
Peptide accession
Q8IXI2
Residue number A
79
Residue number B
147
Peptide name
Mitochondrial Rho GTPase 1
Ligandability
Cysteine 79 of Mitochondrial Rho GTPase 1
Cysteine 147 of Mitochondrial Rho GTPase 1
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