CD59 glycoprotein
Intramolecular
Cysteine 31 and cysteine 38
Cysteine 44 and cysteine 64
Cysteine 70 and cysteine 88
Cysteine 28 and cysteine 51
Cysteine 28 and cysteine 44
Cysteine 89 and cysteine 94
Cysteine 51 and cysteine 94
Cysteine 28 and cysteine 64
Cysteine 44 and cysteine 51
Cysteine 51 and cysteine 89
More...Cysteine 28 and cysteine 94
Cysteine 28 and cysteine 89
Cysteine 51 and cysteine 64
Cysteine 88 and cysteine 89
Cysteine 44 and cysteine 94
Cysteine 70 and cysteine 89
Cysteine 31 and cysteine 44
Cysteine 28 and cysteine 38
Cysteine 38 and cysteine 44
Cysteine 51 and cysteine 70
Cysteine 31 and cysteine 51
Cysteine 88 and cysteine 94
Cysteine 64 and cysteine 70
Cysteine 28 and cysteine 70
Cysteine 28 and cysteine 31
Cysteine 38 and cysteine 64
Cysteine 44 and cysteine 89
Cysteine 44 and cysteine 88
Cysteine 31 and cysteine 64
Cysteine 51 and cysteine 88
Cysteine 28 and cysteine 88
Cysteine 38 and cysteine 51
Cysteine 70 and cysteine 94
Cysteine 64 and cysteine 94
Cysteine 64 and cysteine 88
Cysteine 64 and cysteine 89
5imt D 6 D 13
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 31 and 38 (6 and 13 respectively in this structure).
Details
Redox score ?
87
PDB code
5imt
Structure name
toxin receptor complex
Structure deposition date
2016-03-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
31
Residue number B
38
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 31 of CD59 glycoprotein
Cysteine 38 of CD59 glycoprotein
5imy C 19 C 39
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 44 and 64 (19 and 39 respectively in this structure).
Details
Redox score ?
86
PDB code
5imy
Structure name
trapped toxin
Structure deposition date
2016-03-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
44
Residue number B
64
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 44 of CD59 glycoprotein
Cysteine 64 of CD59 glycoprotein
2ofs A 45 A 63
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 70 and 88 (45 and 63 respectively in this structure).
Details
Redox score ?
85
PDB code
2ofs
Structure name
crystal structure of human cd59
Structure deposition date
2007-01-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
70
Residue number B
88
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 70 of CD59 glycoprotein
Cysteine 88 of CD59 glycoprotein
2ux2 C 3 C 26
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 28 and 51 (3 and 26 respectively in this structure).
Details
Redox score ?
84
PDB code
2ux2
Structure name
high resolution structure of human cd59
Structure deposition date
2007-03-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
28
Residue number B
51
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 28 of CD59 glycoprotein
Cysteine 51 of CD59 glycoprotein
4bik D 3 D 19
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 28 and 44 (3 and 19 respectively in this structure).
Details
Redox score ?
80
PDB code
4bik
Structure name
structure of a disulfide locked mutant of intermedilysin with human cd59
Structure deposition date
2013-04-10
Thiol separation (Å)
3
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
28
Residue number B
44
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 28 of CD59 glycoprotein
Cysteine 44 of CD59 glycoprotein
4bik D 64 D 69
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 89 and 94 (64 and 69 respectively in this structure).
Details
Redox score ?
79
PDB code
4bik
Structure name
structure of a disulfide locked mutant of intermedilysin with human cd59
Structure deposition date
2013-04-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
89
Residue number B
94
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 89 of CD59 glycoprotein
Cysteine 94 of CD59 glycoprotein
2ux2 A 26 A 69
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 51 and 94 (26 and 69 respectively in this structure).
Details
Redox score ?
69
PDB code
2ux2
Structure name
high resolution structure of human cd59
Structure deposition date
2007-03-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
51
Residue number B
94
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 51 of CD59 glycoprotein
Cysteine 94 of CD59 glycoprotein
4bik B 3 B 39
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 28 and 64 (3 and 39 respectively in this structure).
Details
Redox score ?
69
PDB code
4bik
Structure name
structure of a disulfide locked mutant of intermedilysin with human cd59
Structure deposition date
2013-04-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
28
Residue number B
64
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 28 of CD59 glycoprotein
Cysteine 64 of CD59 glycoprotein
5imt D 19 D 26
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 44 and 51 (19 and 26 respectively in this structure).
Details
Redox score ?
65
PDB code
5imt
Structure name
toxin receptor complex
Structure deposition date
2016-03-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
44
Residue number B
51
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 44 of CD59 glycoprotein
Cysteine 51 of CD59 glycoprotein
2ux2 C 26 C 64
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 51 and 89 (26 and 64 respectively in this structure).
Details
Redox score ?
63
PDB code
2ux2
Structure name
high resolution structure of human cd59
Structure deposition date
2007-03-26
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
51
Residue number B
89
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 51 of CD59 glycoprotein
Cysteine 89 of CD59 glycoprotein
4bik B 3 B 69
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 28 and 94 (3 and 69 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
4bik
Structure name
structure of a disulfide locked mutant of intermedilysin with human cd59
Structure deposition date
2013-04-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
28
Residue number B
94
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 28 of CD59 glycoprotein
Cysteine 94 of CD59 glycoprotein
4bik B 3 B 64
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 28 and 89 (3 and 64 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
4bik
Structure name
structure of a disulfide locked mutant of intermedilysin with human cd59
Structure deposition date
2013-04-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
28
Residue number B
89
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 28 of CD59 glycoprotein
Cysteine 89 of CD59 glycoprotein
5imt D 26 D 39
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 51 and 64 (26 and 39 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
5imt
Structure name
toxin receptor complex
Structure deposition date
2016-03-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
51
Residue number B
64
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 51 of CD59 glycoprotein
Cysteine 64 of CD59 glycoprotein
4bik D 63 D 64
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 88 and 89 (63 and 64 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
4bik
Structure name
structure of a disulfide locked mutant of intermedilysin with human cd59
Structure deposition date
2013-04-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
88
Residue number B
89
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 88 of CD59 glycoprotein
Cysteine 89 of CD59 glycoprotein
4bik D 19 D 69
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 44 and 94 (19 and 69 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
4bik
Structure name
structure of a disulfide locked mutant of intermedilysin with human cd59
Structure deposition date
2013-04-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
44
Residue number B
94
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 44 of CD59 glycoprotein
Cysteine 94 of CD59 glycoprotein
2ofs A 45 A 64
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 70 and 89 (45 and 64 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
2ofs
Structure name
crystal structure of human cd59
Structure deposition date
2007-01-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
70
Residue number B
89
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 70 of CD59 glycoprotein
Cysteine 89 of CD59 glycoprotein
1cdr A 6 A 19
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 31 and 44 (6 and 19 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
1cdr
Structure name
structure of a soluble, glycosylated form of the human complement regulatory protein cd59
Structure deposition date
1994-06-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
31
Residue number B
44
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 31 of CD59 glycoprotein
Cysteine 44 of CD59 glycoprotein
5imy C 3 C 13
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 28 and 38 (3 and 13 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
5imy
Structure name
trapped toxin
Structure deposition date
2016-03-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
28
Residue number B
38
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 28 of CD59 glycoprotein
Cysteine 38 of CD59 glycoprotein
1cdq A 13 A 19
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 38 and 44 (13 and 19 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
1cdq
Structure name
structure of a soluble, glycosylated form of the human complement regulatory protein cd59
Structure deposition date
1994-06-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
38
Residue number B
44
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 38 of CD59 glycoprotein
Cysteine 44 of CD59 glycoprotein
5imy D 26 D 45
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 51 and 70 (26 and 45 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
5imy
Structure name
trapped toxin
Structure deposition date
2016-03-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
51
Residue number B
70
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 51 of CD59 glycoprotein
Cysteine 70 of CD59 glycoprotein
1cdq A 6 A 26
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 31 and 51 (6 and 26 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
1cdq
Structure name
structure of a soluble, glycosylated form of the human complement regulatory protein cd59
Structure deposition date
1994-06-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
31
Residue number B
51
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 31 of CD59 glycoprotein
Cysteine 51 of CD59 glycoprotein
2ofs A 63 A 69
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 88 and 94 (63 and 69 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
2ofs
Structure name
crystal structure of human cd59
Structure deposition date
2007-01-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
88
Residue number B
94
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 88 of CD59 glycoprotein
Cysteine 94 of CD59 glycoprotein
1cdq A 39 A 45
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 64 and 70 (39 and 45 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
1cdq
Structure name
structure of a soluble, glycosylated form of the human complement regulatory protein cd59
Structure deposition date
1994-06-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
64
Residue number B
70
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 64 of CD59 glycoprotein
Cysteine 70 of CD59 glycoprotein
4bik D 3 D 45
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 28 and 70 (3 and 45 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
4bik
Structure name
structure of a disulfide locked mutant of intermedilysin with human cd59
Structure deposition date
2013-04-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
28
Residue number B
70
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 28 of CD59 glycoprotein
Cysteine 70 of CD59 glycoprotein
1cdq A 3 A 6
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 28 and 31 (3 and 6 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
1cdq
Structure name
structure of a soluble, glycosylated form of the human complement regulatory protein cd59
Structure deposition date
1994-06-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
28
Residue number B
31
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 28 of CD59 glycoprotein
Cysteine 31 of CD59 glycoprotein
2ux2 A 13 A 39
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 38 and 64 (13 and 39 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
2ux2
Structure name
high resolution structure of human cd59
Structure deposition date
2007-03-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
38
Residue number B
64
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 38 of CD59 glycoprotein
Cysteine 64 of CD59 glycoprotein
4bik D 19 D 64
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 44 and 89 (19 and 64 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
4bik
Structure name
structure of a disulfide locked mutant of intermedilysin with human cd59
Structure deposition date
2013-04-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
44
Residue number B
89
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 44 of CD59 glycoprotein
Cysteine 89 of CD59 glycoprotein
1cdr A 19 A 63
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 44 and 88 (19 and 63 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
1cdr
Structure name
structure of a soluble, glycosylated form of the human complement regulatory protein cd59
Structure deposition date
1994-06-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
44
Residue number B
88
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 44 of CD59 glycoprotein
Cysteine 88 of CD59 glycoprotein
1cds A 6 A 39
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 31 and 64 (6 and 39 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
1cds
Structure name
structure of a soluble, glycosylated form of the human complement regulatory protein cd59
Structure deposition date
1994-06-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
31
Residue number B
64
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 31 of CD59 glycoprotein
Cysteine 64 of CD59 glycoprotein
2ux2 A 26 A 63
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 51 and 88 (26 and 63 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
2ux2
Structure name
high resolution structure of human cd59
Structure deposition date
2007-03-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
51
Residue number B
88
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 51 of CD59 glycoprotein
Cysteine 88 of CD59 glycoprotein
4bik D 3 D 63
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 28 and 88 (3 and 63 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
4bik
Structure name
structure of a disulfide locked mutant of intermedilysin with human cd59
Structure deposition date
2013-04-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
28
Residue number B
88
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 28 of CD59 glycoprotein
Cysteine 88 of CD59 glycoprotein
1cds A 13 A 26
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 38 and 51 (13 and 26 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
1cds
Structure name
structure of a soluble, glycosylated form of the human complement regulatory protein cd59
Structure deposition date
1994-06-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
38
Residue number B
51
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 38 of CD59 glycoprotein
Cysteine 51 of CD59 glycoprotein
2ux2 A 45 A 69
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 70 and 94 (45 and 69 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
2ux2
Structure name
high resolution structure of human cd59
Structure deposition date
2007-03-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
70
Residue number B
94
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 70 of CD59 glycoprotein
Cysteine 94 of CD59 glycoprotein
4bik D 39 D 69
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 64 and 94 (39 and 69 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
4bik
Structure name
structure of a disulfide locked mutant of intermedilysin with human cd59
Structure deposition date
2013-04-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
64
Residue number B
94
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 64 of CD59 glycoprotein
Cysteine 94 of CD59 glycoprotein
1cdr A 39 A 63
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 64 and 88 (39 and 63 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
1cdr
Structure name
structure of a soluble, glycosylated form of the human complement regulatory protein cd59
Structure deposition date
1994-06-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
64
Residue number B
88
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 64 of CD59 glycoprotein
Cysteine 88 of CD59 glycoprotein
4bik D 39 D 64
A redox-regulated disulphide may form within CD59 glycoprotein between cysteines 64 and 89 (39 and 64 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
4bik
Structure name
structure of a disulfide locked mutant of intermedilysin with human cd59
Structure deposition date
2013-04-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13987
Residue number A
64
Residue number B
89
Peptide name
CD59 glycoprotein
Ligandability
Cysteine 64 of CD59 glycoprotein
Cysteine 89 of CD59 glycoprotein
If this tool was useful for finding a disulphide, please cite: