Rho-related GTP-binding protein RhoG
Intramolecular
Cysteine 22 and cysteine 157 L
Cysteine 102 and cysteine 105
Cysteine 18 and cysteine 22 L
Cysteine 81 and cysteine 157 L
Cysteine 6 and cysteine 81
6uka A 22 A 157
A redox-regulated disulphide may form within Rho-related GTP-binding protein RhoG between cysteines 22 and 157. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
6uka
Structure name
crystal structure of rhog and elmo complex
Structure deposition date
2019-10-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
64
Peptide accession
P84095
Residue number A
22
Residue number B
157
Peptide name
Rho-related GTP-binding protein RhoG
Ligandability
Cysteine 22 of Rho-related GTP-binding protein RhoG
Cysteine 157 of Rho-related GTP-binding protein RhoG
6uka A 102 A 105
A redox-regulated disulphide may form within Rho-related GTP-binding protein RhoG between cysteines 102 and 105. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
6uka
Structure name
crystal structure of rhog and elmo complex
Structure deposition date
2019-10-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
18
Peptide accession
P84095
Residue number A
102
Residue number B
105
Peptide name
Rho-related GTP-binding protein RhoG
Ligandability
Cysteine 102 of Rho-related GTP-binding protein RhoG
Cysteine 105 of Rho-related GTP-binding protein RhoG
6uka A 18 A 22
A redox-regulated disulphide may form within Rho-related GTP-binding protein RhoG between cysteines 18 and 22. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
6uka
Structure name
crystal structure of rhog and elmo complex
Structure deposition date
2019-10-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
44
Peptide accession
P84095
Residue number A
18
Residue number B
22
Peptide name
Rho-related GTP-binding protein RhoG
Ligandability
Cysteine 18 of Rho-related GTP-binding protein RhoG
Cysteine 22 of Rho-related GTP-binding protein RhoG
6uka A 81 A 157
A redox-regulated disulphide may form within Rho-related GTP-binding protein RhoG between cysteines 81 and 157. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
6uka
Structure name
crystal structure of rhog and elmo complex
Structure deposition date
2019-10-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
89
Minimum pKa ?
13
% buried
100
Peptide accession
P84095
Residue number A
81
Residue number B
157
Peptide name
Rho-related GTP-binding protein RhoG
Ligandability
Cysteine 81 of Rho-related GTP-binding protein RhoG
Cysteine 157 of Rho-related GTP-binding protein RhoG
6uka A 6 A 81
A redox-regulated disulphide may form within Rho-related GTP-binding protein RhoG between cysteines 6 and 81. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
6uka
Structure name
crystal structure of rhog and elmo complex
Structure deposition date
2019-10-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
95
Minimum pKa ?
12
% buried
100
Peptide accession
P84095
Residue number A
6
Residue number B
81
Peptide name
Rho-related GTP-binding protein RhoG
Ligandability
Cysteine 6 of Rho-related GTP-binding protein RhoG
Cysteine 81 of Rho-related GTP-binding protein RhoG
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