Glypican-1
Intramolecular
Cysteine 191 and cysteine 343
Cysteine 32 and cysteine 68
Cysteine 62 and cysteine 256
Cysteine 268 and cysteine 415
Cysteine 272 and cysteine 401
Cysteine 246 and cysteine 279
Cysteine 69 and cysteine 259
Cysteine 62 and cysteine 259
Cysteine 62 and cysteine 69
Cysteine 256 and cysteine 259
More...Cysteine 68 and cysteine 69
Cysteine 32 and cysteine 69
Cysteine 69 and cysteine 256
Cysteine 68 and cysteine 259
Cysteine 32 and cysteine 259
Cysteine 272 and cysteine 279
Cysteine 268 and cysteine 272
Cysteine 279 and cysteine 401
4bwe B 191 B 343
A redox-regulated disulphide may form within Glypican-1 between cysteines 191 and 343.
Details
Redox score ?
84
PDB code
4bwe
Structure name
crystal structure of c-terminally truncated glypican-1 after controlled dehydration to 86 percent relative humidity
Structure deposition date
2013-07-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35052
Residue number A
191
Residue number B
343
Peptide name
Glypican-1
Ligandability
Cysteine 191 of Glypican-1
Cysteine 343 of Glypican-1
4bwe A 32 A 68
A redox-regulated disulphide may form within Glypican-1 between cysteines 32 and 68.
Details
Redox score ?
84
PDB code
4bwe
Structure name
crystal structure of c-terminally truncated glypican-1 after controlled dehydration to 86 percent relative humidity
Structure deposition date
2013-07-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35052
Residue number A
32
Residue number B
68
Peptide name
Glypican-1
Ligandability
Cysteine 32 of Glypican-1
Cysteine 68 of Glypican-1
4bwe A 62 A 256
A redox-regulated disulphide may form within Glypican-1 between cysteines 62 and 256.
Details
Redox score ?
83
PDB code
4bwe
Structure name
crystal structure of c-terminally truncated glypican-1 after controlled dehydration to 86 percent relative humidity
Structure deposition date
2013-07-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35052
Residue number A
62
Residue number B
256
Peptide name
Glypican-1
Ligandability
Cysteine 62 of Glypican-1
Cysteine 256 of Glypican-1
4acr D 268 D 415
A redox-regulated disulphide may form within Glypican-1 between cysteines 268 and 415.
Details
Redox score ?
83
PDB code
4acr
Structure name
crystal structure of n-glycosylated, c-terminally truncated human glypican-1
Structure deposition date
2011-12-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35052
Residue number A
268
Residue number B
415
Peptide name
Glypican-1
Ligandability
Cysteine 268 of Glypican-1
Cysteine 415 of Glypican-1
4bwe B 272 B 401
A redox-regulated disulphide may form within Glypican-1 between cysteines 272 and 401.
Details
Redox score ?
82
PDB code
4bwe
Structure name
crystal structure of c-terminally truncated glypican-1 after controlled dehydration to 86 percent relative humidity
Structure deposition date
2013-07-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35052
Residue number A
272
Residue number B
401
Peptide name
Glypican-1
Ligandability
Cysteine 272 of Glypican-1
Cysteine 401 of Glypican-1
4ad7 A 246 A 279
A redox-regulated disulphide may form within Glypican-1 between cysteines 246 and 279.
Details
Redox score ?
81
PDB code
4ad7
Structure name
crystal structure of full-length n-glycosylated human glypican-1
Structure deposition date
2011-12-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35052
Residue number A
246
Residue number B
279
Peptide name
Glypican-1
Ligandability
Cysteine 246 of Glypican-1
Cysteine 279 of Glypican-1
4ad7 A 69 A 259
A redox-regulated disulphide may form within Glypican-1 between cysteines 69 and 259.
Details
Redox score ?
80
PDB code
4ad7
Structure name
crystal structure of full-length n-glycosylated human glypican-1
Structure deposition date
2011-12-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
97
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35052
Residue number A
69
Residue number B
259
Peptide name
Glypican-1
Ligandability
Cysteine 69 of Glypican-1
Cysteine 259 of Glypican-1
4acr B 62 B 259
A redox-regulated disulphide may form within Glypican-1 between cysteines 62 and 259.
Details
Redox score ?
69
PDB code
4acr
Structure name
crystal structure of n-glycosylated, c-terminally truncated human glypican-1
Structure deposition date
2011-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35052
Residue number A
62
Residue number B
259
Peptide name
Glypican-1
Ligandability
Cysteine 62 of Glypican-1
Cysteine 259 of Glypican-1
4ad7 C 62 C 69
A redox-regulated disulphide may form within Glypican-1 between cysteines 62 and 69.
Details
Redox score ?
60
PDB code
4ad7
Structure name
crystal structure of full-length n-glycosylated human glypican-1
Structure deposition date
2011-12-22
Thiol separation (Å)
6
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35052
Residue number A
62
Residue number B
69
Peptide name
Glypican-1
Ligandability
Cysteine 62 of Glypican-1
Cysteine 69 of Glypican-1
4ad7 A 256 A 259
A redox-regulated disulphide may form within Glypican-1 between cysteines 256 and 259. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
4ad7
Structure name
crystal structure of full-length n-glycosylated human glypican-1
Structure deposition date
2011-12-22
Thiol separation (Å)
6
Half-sphere exposure sum ?
99
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35052
Residue number A
256
Residue number B
259
Peptide name
Glypican-1
Ligandability
Cysteine 256 of Glypican-1
Cysteine 259 of Glypican-1
4ad7 B 68 B 69
A redox-regulated disulphide may form within Glypican-1 between cysteines 68 and 69. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
4ad7
Structure name
crystal structure of full-length n-glycosylated human glypican-1
Structure deposition date
2011-12-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35052
Residue number A
68
Residue number B
69
Peptide name
Glypican-1
Ligandability
Cysteine 68 of Glypican-1
Cysteine 69 of Glypican-1
4ad7 B 32 B 69
A redox-regulated disulphide may form within Glypican-1 between cysteines 32 and 69. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
4ad7
Structure name
crystal structure of full-length n-glycosylated human glypican-1
Structure deposition date
2011-12-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35052
Residue number A
32
Residue number B
69
Peptide name
Glypican-1
Ligandability
Cysteine 32 of Glypican-1
Cysteine 69 of Glypican-1
4ad7 A 69 A 256
A redox-regulated disulphide may form within Glypican-1 between cysteines 69 and 256. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
4ad7
Structure name
crystal structure of full-length n-glycosylated human glypican-1
Structure deposition date
2011-12-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35052
Residue number A
69
Residue number B
256
Peptide name
Glypican-1
Ligandability
Cysteine 69 of Glypican-1
Cysteine 256 of Glypican-1
4ad7 C 68 C 259
A redox-regulated disulphide may form within Glypican-1 between cysteines 68 and 259. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
4ad7
Structure name
crystal structure of full-length n-glycosylated human glypican-1
Structure deposition date
2011-12-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35052
Residue number A
68
Residue number B
259
Peptide name
Glypican-1
Ligandability
Cysteine 68 of Glypican-1
Cysteine 259 of Glypican-1
4acr B 32 B 259
A redox-regulated disulphide may form within Glypican-1 between cysteines 32 and 259. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
4acr
Structure name
crystal structure of n-glycosylated, c-terminally truncated human glypican-1
Structure deposition date
2011-12-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35052
Residue number A
32
Residue number B
259
Peptide name
Glypican-1
Ligandability
Cysteine 32 of Glypican-1
Cysteine 259 of Glypican-1
4ad7 A 272 A 279
A redox-regulated disulphide may form within Glypican-1 between cysteines 272 and 279. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
4ad7
Structure name
crystal structure of full-length n-glycosylated human glypican-1
Structure deposition date
2011-12-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35052
Residue number A
272
Residue number B
279
Peptide name
Glypican-1
Ligandability
Cysteine 272 of Glypican-1
Cysteine 279 of Glypican-1
4ad7 B 268 B 272
A redox-regulated disulphide may form within Glypican-1 between cysteines 268 and 272. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
4ad7
Structure name
crystal structure of full-length n-glycosylated human glypican-1
Structure deposition date
2011-12-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35052
Residue number A
268
Residue number B
272
Peptide name
Glypican-1
Ligandability
Cysteine 268 of Glypican-1
Cysteine 272 of Glypican-1
4bwe A 279 A 401
A redox-regulated disulphide may form within Glypican-1 between cysteines 279 and 401. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
4bwe
Structure name
crystal structure of c-terminally truncated glypican-1 after controlled dehydration to 86 percent relative humidity
Structure deposition date
2013-07-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35052
Residue number A
279
Residue number B
401
Peptide name
Glypican-1
Ligandability
Cysteine 279 of Glypican-1
Cysteine 401 of Glypican-1
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