Ephrin type-A receptor 7
Intramolecular
Cysteine 109 and cysteine 119
Cysteine 74 and cysteine 192
Cysteine 74 and cysteine 119
Cysteine 119 and cysteine 192
Cysteine 74 and cysteine 109
Cysteine 109 and cysteine 192
3nru J 109 J 119
A redox-regulated disulphide may form within Ephrin type-A receptor 7 between cysteines 109 and 119.
Details
Redox score ?
87
PDB code
3nru
Structure name
ligand binding domain of epha7
Structure deposition date
2010-06-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLK0
Residue number A
109
Residue number B
119
Peptide name
Ephrin type-A receptor 7
Ligandability
Cysteine 109 of Ephrin type-A receptor 7
Cysteine 119 of Ephrin type-A receptor 7
3nru I 74 I 192
A redox-regulated disulphide may form within Ephrin type-A receptor 7 between cysteines 74 and 192.
Details
Redox score ?
75
PDB code
3nru
Structure name
ligand binding domain of epha7
Structure deposition date
2010-06-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
67
Minimum pKa ?
9
% buried
31
Peptide accession
B7ZLK0
Residue number A
74
Residue number B
192
Peptide name
Ephrin type-A receptor 7
Ligandability
Cysteine 74 of Ephrin type-A receptor 7
Cysteine 192 of Ephrin type-A receptor 7
3nru G 74 G 119
A redox-regulated disulphide may form within Ephrin type-A receptor 7 between cysteines 74 and 119. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
3nru
Structure name
ligand binding domain of epha7
Structure deposition date
2010-06-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLK0
Residue number A
74
Residue number B
119
Peptide name
Ephrin type-A receptor 7
Ligandability
Cysteine 74 of Ephrin type-A receptor 7
Cysteine 119 of Ephrin type-A receptor 7
3nru G 119 G 192
A redox-regulated disulphide may form within Ephrin type-A receptor 7 between cysteines 119 and 192. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
3nru
Structure name
ligand binding domain of epha7
Structure deposition date
2010-06-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLK0
Residue number A
119
Residue number B
192
Peptide name
Ephrin type-A receptor 7
Ligandability
Cysteine 119 of Ephrin type-A receptor 7
Cysteine 192 of Ephrin type-A receptor 7
3nru A 74 A 109
A redox-regulated disulphide may form within Ephrin type-A receptor 7 between cysteines 74 and 109. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
3nru
Structure name
ligand binding domain of epha7
Structure deposition date
2010-06-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLK0
Residue number A
74
Residue number B
109
Peptide name
Ephrin type-A receptor 7
Ligandability
Cysteine 74 of Ephrin type-A receptor 7
Cysteine 109 of Ephrin type-A receptor 7
3nru E 109 E 192
A redox-regulated disulphide may form within Ephrin type-A receptor 7 between cysteines 109 and 192. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
3nru
Structure name
ligand binding domain of epha7
Structure deposition date
2010-06-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
B7ZLK0
Residue number A
109
Residue number B
192
Peptide name
Ephrin type-A receptor 7
Ligandability
Cysteine 109 of Ephrin type-A receptor 7
Cysteine 192 of Ephrin type-A receptor 7
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