Protein SEC13 homolog
Intermolecular
Cysteine 299 and cysteine 299
Intramolecular
Cysteine 153 and cysteine 187 L
Cysteine 77 and cysteine 122
Cysteine 31 and cysteine 77
Cysteine 110 and cysteine 122
Cysteine 122 and cysteine 153
Cysteine 77 and cysteine 153
3bg1 A 299 E 299
A redox-regulated disulphide may form between two units of Protein SEC13 homolog at cysteines 299 and 299. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
3bg1
Structure name
architecture of a coat for the nuclear pore membrane
Structure deposition date
2007-11-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
12
% buried
94
Peptide A name
Protein SEC13 homolog
Peptide B name
Protein SEC13 homolog
Peptide A accession
P55735
Peptide B accession
P55735
Peptide A residue number
299
Peptide B residue number
299
Ligandability
3bg0 D 153 D 187
A redox-regulated disulphide may form within Protein SEC13 homolog between cysteines 153 and 187. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
3bg0
Structure name
architecture of a coat for the nuclear pore membrane
Structure deposition date
2007-11-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
11
% buried
88
Peptide accession
P55735
Residue number A
153
Residue number B
187
Peptide name
Protein SEC13 homolog
Ligandability
Cysteine 153 of Protein SEC13 homolog
Cysteine 187 of Protein SEC13 homolog
3bg1 D 77 D 122
A redox-regulated disulphide may form within Protein SEC13 homolog between cysteines 77 and 122. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
3bg1
Structure name
architecture of a coat for the nuclear pore membrane
Structure deposition date
2007-11-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
107
Minimum pKa ?
12
% buried
100
Peptide accession
P55735
Residue number A
77
Residue number B
122
Peptide name
Protein SEC13 homolog
Ligandability
Cysteine 77 of Protein SEC13 homolog
Cysteine 122 of Protein SEC13 homolog
3bg1 A 31 A 77
A redox-regulated disulphide may form within Protein SEC13 homolog between cysteines 31 and 77. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
3bg1
Structure name
architecture of a coat for the nuclear pore membrane
Structure deposition date
2007-11-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
91
Minimum pKa ?
13
% buried
100
Peptide accession
P55735
Residue number A
31
Residue number B
77
Peptide name
Protein SEC13 homolog
Ligandability
Cysteine 31 of Protein SEC13 homolog
Cysteine 77 of Protein SEC13 homolog
3bg0 A 110 A 122
A redox-regulated disulphide may form within Protein SEC13 homolog between cysteines 110 and 122. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
3bg0
Structure name
architecture of a coat for the nuclear pore membrane
Structure deposition date
2007-11-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
99
Minimum pKa ?
11
% buried
100
Peptide accession
P55735
Residue number A
110
Residue number B
122
Peptide name
Protein SEC13 homolog
Ligandability
Cysteine 110 of Protein SEC13 homolog
Cysteine 122 of Protein SEC13 homolog
3bg1 A 122 A 153
A redox-regulated disulphide may form within Protein SEC13 homolog between cysteines 122 and 153. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
3bg1
Structure name
architecture of a coat for the nuclear pore membrane
Structure deposition date
2007-11-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
100
Minimum pKa ?
12
% buried
100
Peptide accession
P55735
Residue number A
122
Residue number B
153
Peptide name
Protein SEC13 homolog
Ligandability
Cysteine 122 of Protein SEC13 homolog
Cysteine 153 of Protein SEC13 homolog
3bg1 D 77 D 153
A redox-regulated disulphide may form within Protein SEC13 homolog between cysteines 77 and 153. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
23
PDB code
3bg1
Structure name
architecture of a coat for the nuclear pore membrane
Structure deposition date
2007-11-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
96
Minimum pKa ?
13
% buried
100
Peptide accession
P55735
Residue number A
77
Residue number B
153
Peptide name
Protein SEC13 homolog
Ligandability
Cysteine 77 of Protein SEC13 homolog
Cysteine 153 of Protein SEC13 homolog
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