Rho-related GTP-binding protein RhoD
Intramolecular
Cysteine 129 and cysteine 171
Cysteine 95 and cysteine 129
Cysteine 28 and cysteine 129
Cysteine 28 and cysteine 95
Cysteine 95 and cysteine 171
Cysteine 28 and cysteine 171
2j1l A 129 A 171
A redox-regulated disulphide may form within Rho-related GTP-binding protein RhoD between cysteines 129 and 171.
Details
Redox score ?
71
PDB code
2j1l
Structure name
crystal structure of human rho-related gtp-binding protein rhod
Structure deposition date
2006-08-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
84
Minimum pKa ?
5
% buried
96
Peptide accession
O00212
Residue number A
129
Residue number B
171
Peptide name
Rho-related GTP-binding protein RhoD
Ligandability
Cysteine 129 of Rho-related GTP-binding protein RhoD
Cysteine 171 of Rho-related GTP-binding protein RhoD
2j1l A 95 A 129
A redox-regulated disulphide may form within Rho-related GTP-binding protein RhoD between cysteines 95 and 129.
Details
Redox score ?
70
PDB code
2j1l
Structure name
crystal structure of human rho-related gtp-binding protein rhod
Structure deposition date
2006-08-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
94
Minimum pKa ?
5
% buried
100
Peptide accession
O00212
Residue number A
95
Residue number B
129
Peptide name
Rho-related GTP-binding protein RhoD
Ligandability
Cysteine 95 of Rho-related GTP-binding protein RhoD
Cysteine 129 of Rho-related GTP-binding protein RhoD
7kdc A 28 A 129
A redox-regulated disulphide may form within Rho-related GTP-binding protein RhoD between cysteines 28 and 129.
Details
Redox score ?
68
PDB code
7kdc
Structure name
the complex between rhod and the plexin b2 rbd
Structure deposition date
2020-10-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
87
Minimum pKa ?
4
% buried
100
Peptide accession
O00212
Residue number A
28
Residue number B
129
Peptide name
Rho-related GTP-binding protein RhoD
Ligandability
Cysteine 28 of Rho-related GTP-binding protein RhoD
Cysteine 129 of Rho-related GTP-binding protein RhoD
7kdc B 28 B 95
A redox-regulated disulphide may form within Rho-related GTP-binding protein RhoD between cysteines 28 and 95. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
7kdc
Structure name
the complex between rhod and the plexin b2 rbd
Structure deposition date
2020-10-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
88
Minimum pKa ?
13
% buried
100
Peptide accession
O00212
Residue number A
28
Residue number B
95
Peptide name
Rho-related GTP-binding protein RhoD
Ligandability
Cysteine 28 of Rho-related GTP-binding protein RhoD
Cysteine 95 of Rho-related GTP-binding protein RhoD
7kdc B 95 B 171
A redox-regulated disulphide may form within Rho-related GTP-binding protein RhoD between cysteines 95 and 171. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
7kdc
Structure name
the complex between rhod and the plexin b2 rbd
Structure deposition date
2020-10-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
18
% buried
99
Peptide accession
O00212
Residue number A
95
Residue number B
171
Peptide name
Rho-related GTP-binding protein RhoD
Ligandability
Cysteine 95 of Rho-related GTP-binding protein RhoD
Cysteine 171 of Rho-related GTP-binding protein RhoD
7kdc A 28 A 171
A redox-regulated disulphide may form within Rho-related GTP-binding protein RhoD between cysteines 28 and 171. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
22
PDB code
7kdc
Structure name
the complex between rhod and the plexin b2 rbd
Structure deposition date
2020-10-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
15
% buried
99
Peptide accession
O00212
Residue number A
28
Residue number B
171
Peptide name
Rho-related GTP-binding protein RhoD
Ligandability
Cysteine 28 of Rho-related GTP-binding protein RhoD
Cysteine 171 of Rho-related GTP-binding protein RhoD
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