R-spondin-2
Intramolecular
Cysteine 128 and cysteine 141
Cysteine 40 and cysteine 46
Cysteine 78 and cysteine 93
Cysteine 101 and cysteine 110
Cysteine 96 and cysteine 104
Cysteine 43 and cysteine 52
Cysteine 55 and cysteine 74
Cysteine 113 and cysteine 124
Cysteine 40 and cysteine 43
Cysteine 110 and cysteine 124
More...Cysteine 52 and cysteine 55
Cysteine 101 and cysteine 124
Cysteine 104 and cysteine 110
Cysteine 52 and cysteine 74
Cysteine 96 and cysteine 101
Cysteine 101 and cysteine 104
Cysteine 43 and cysteine 46
Cysteine 40 and cysteine 52
Cysteine 110 and cysteine 113
Cysteine 43 and cysteine 74
Cysteine 96 and cysteine 110
Cysteine 101 and cysteine 113
Cysteine 46 and cysteine 52
Cysteine 43 and cysteine 55
Cysteine 40 and cysteine 74
Cysteine 40 and cysteine 55
Cysteine 113 and cysteine 141
Cysteine 78 and cysteine 96
Cysteine 113 and cysteine 128
Cysteine 55 and cysteine 78
Cysteine 55 and cysteine 93
Cysteine 46 and cysteine 74
Cysteine 104 and cysteine 124
Cysteine 78 and cysteine 104
Cysteine 74 and cysteine 93
Cysteine 124 and cysteine 141
Cysteine 93 and cysteine 96
Cysteine 96 and cysteine 124
4c99 D 128 D 141
A redox-regulated disulphide may form within R-spondin-2 between cysteines 128 and 141.
Details
Redox score ?
90
PDB code
4c99
Structure name
mouse znrf3 ectodomain in complex with mouse rspo2 fu1-fu2 crystal form i
Structure deposition date
2013-10-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
128
Residue number B
141
Peptide name
R-spondin-2
Ligandability
Cysteine 128 of R-spondin-2
Cysteine 141 of R-spondin-2
4c99 B 40 B 46
A redox-regulated disulphide may form within R-spondin-2 between cysteines 40 and 46.
Details
Redox score ?
88
PDB code
4c99
Structure name
mouse znrf3 ectodomain in complex with mouse rspo2 fu1-fu2 crystal form i
Structure deposition date
2013-10-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
40
Residue number B
46
Peptide name
R-spondin-2
Ligandability
Cysteine 40 of R-spondin-2
Cysteine 46 of R-spondin-2
4ufs B 78 B 93
A redox-regulated disulphide may form within R-spondin-2 between cysteines 78 and 93.
Details
Redox score ?
87
PDB code
4ufs
Structure name
low resolution structure r-spondin-2 (fu1fu2) in complex with the ectodomains of lgr5 and znrf3
Structure deposition date
2015-03-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
78
Residue number B
93
Peptide name
R-spondin-2
Ligandability
Cysteine 78 of R-spondin-2
Cysteine 93 of R-spondin-2
4c99 B 101 B 110
A redox-regulated disulphide may form within R-spondin-2 between cysteines 101 and 110.
Details
Redox score ?
87
PDB code
4c99
Structure name
mouse znrf3 ectodomain in complex with mouse rspo2 fu1-fu2 crystal form i
Structure deposition date
2013-10-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
101
Residue number B
110
Peptide name
R-spondin-2
Ligandability
Cysteine 101 of R-spondin-2
Cysteine 110 of R-spondin-2
4ufs B 96 B 104
A redox-regulated disulphide may form within R-spondin-2 between cysteines 96 and 104.
Details
Redox score ?
87
PDB code
4ufs
Structure name
low resolution structure r-spondin-2 (fu1fu2) in complex with the ectodomains of lgr5 and znrf3
Structure deposition date
2015-03-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
96
Residue number B
104
Peptide name
R-spondin-2
Ligandability
Cysteine 96 of R-spondin-2
Cysteine 104 of R-spondin-2
4ufr D 43 D 52
A redox-regulated disulphide may form within R-spondin-2 between cysteines 43 and 52.
Details
Redox score ?
86
PDB code
4ufr
Structure name
structure of the ectodomain of lgr5 in complex with r-spondin-2 (fu1fu2)
Structure deposition date
2015-03-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
43
Residue number B
52
Peptide name
R-spondin-2
Ligandability
Cysteine 43 of R-spondin-2
Cysteine 52 of R-spondin-2
4ufs B 55 B 74
A redox-regulated disulphide may form within R-spondin-2 between cysteines 55 and 74.
Details
Redox score ?
86
PDB code
4ufs
Structure name
low resolution structure r-spondin-2 (fu1fu2) in complex with the ectodomains of lgr5 and znrf3
Structure deposition date
2015-03-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
55
Residue number B
74
Peptide name
R-spondin-2
Ligandability
Cysteine 55 of R-spondin-2
Cysteine 74 of R-spondin-2
4ufr B 113 B 124
A redox-regulated disulphide may form within R-spondin-2 between cysteines 113 and 124.
Details
Redox score ?
85
PDB code
4ufr
Structure name
structure of the ectodomain of lgr5 in complex with r-spondin-2 (fu1fu2)
Structure deposition date
2015-03-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
113
Residue number B
124
Peptide name
R-spondin-2
Ligandability
Cysteine 113 of R-spondin-2
Cysteine 124 of R-spondin-2
4ufr D 40 D 43
A redox-regulated disulphide may form within R-spondin-2 between cysteines 40 and 43.
Details
Redox score ?
78
PDB code
4ufr
Structure name
structure of the ectodomain of lgr5 in complex with r-spondin-2 (fu1fu2)
Structure deposition date
2015-03-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
40
Residue number B
43
Peptide name
R-spondin-2
Ligandability
Cysteine 40 of R-spondin-2
Cysteine 43 of R-spondin-2
4ufr B 110 B 124
A redox-regulated disulphide may form within R-spondin-2 between cysteines 110 and 124.
Details
Redox score ?
75
PDB code
4ufr
Structure name
structure of the ectodomain of lgr5 in complex with r-spondin-2 (fu1fu2)
Structure deposition date
2015-03-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
110
Residue number B
124
Peptide name
R-spondin-2
Ligandability
Cysteine 110 of R-spondin-2
Cysteine 124 of R-spondin-2
4ufr B 52 B 55
A redox-regulated disulphide may form within R-spondin-2 between cysteines 52 and 55.
Details
Redox score ?
74
PDB code
4ufr
Structure name
structure of the ectodomain of lgr5 in complex with r-spondin-2 (fu1fu2)
Structure deposition date
2015-03-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
52
Residue number B
55
Peptide name
R-spondin-2
Ligandability
Cysteine 52 of R-spondin-2
Cysteine 55 of R-spondin-2
4c99 B 101 B 124
A redox-regulated disulphide may form within R-spondin-2 between cysteines 101 and 124.
Details
Redox score ?
73
PDB code
4c99
Structure name
mouse znrf3 ectodomain in complex with mouse rspo2 fu1-fu2 crystal form i
Structure deposition date
2013-10-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
101
Residue number B
124
Peptide name
R-spondin-2
Ligandability
Cysteine 101 of R-spondin-2
Cysteine 124 of R-spondin-2
4c99 B 104 B 110
A redox-regulated disulphide may form within R-spondin-2 between cysteines 104 and 110.
Details
Redox score ?
72
PDB code
4c99
Structure name
mouse znrf3 ectodomain in complex with mouse rspo2 fu1-fu2 crystal form i
Structure deposition date
2013-10-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
104
Residue number B
110
Peptide name
R-spondin-2
Ligandability
Cysteine 104 of R-spondin-2
Cysteine 110 of R-spondin-2
4c99 D 52 D 74
A redox-regulated disulphide may form within R-spondin-2 between cysteines 52 and 74.
Details
Redox score ?
72
PDB code
4c99
Structure name
mouse znrf3 ectodomain in complex with mouse rspo2 fu1-fu2 crystal form i
Structure deposition date
2013-10-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
52
Residue number B
74
Peptide name
R-spondin-2
Ligandability
Cysteine 52 of R-spondin-2
Cysteine 74 of R-spondin-2
4c99 D 96 D 101
A redox-regulated disulphide may form within R-spondin-2 between cysteines 96 and 101.
Details
Redox score ?
72
PDB code
4c99
Structure name
mouse znrf3 ectodomain in complex with mouse rspo2 fu1-fu2 crystal form i
Structure deposition date
2013-10-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
96
Residue number B
101
Peptide name
R-spondin-2
Ligandability
Cysteine 96 of R-spondin-2
Cysteine 101 of R-spondin-2
4c99 D 101 D 104
A redox-regulated disulphide may form within R-spondin-2 between cysteines 101 and 104.
Details
Redox score ?
72
PDB code
4c99
Structure name
mouse znrf3 ectodomain in complex with mouse rspo2 fu1-fu2 crystal form i
Structure deposition date
2013-10-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
101
Residue number B
104
Peptide name
R-spondin-2
Ligandability
Cysteine 101 of R-spondin-2
Cysteine 104 of R-spondin-2
4ufr B 43 B 46
A redox-regulated disulphide may form within R-spondin-2 between cysteines 43 and 46.
Details
Redox score ?
70
PDB code
4ufr
Structure name
structure of the ectodomain of lgr5 in complex with r-spondin-2 (fu1fu2)
Structure deposition date
2015-03-18
Thiol separation (Å)
5
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
43
Residue number B
46
Peptide name
R-spondin-2
Ligandability
Cysteine 43 of R-spondin-2
Cysteine 46 of R-spondin-2
4ufr D 40 D 52
A redox-regulated disulphide may form within R-spondin-2 between cysteines 40 and 52.
Details
Redox score ?
70
PDB code
4ufr
Structure name
structure of the ectodomain of lgr5 in complex with r-spondin-2 (fu1fu2)
Structure deposition date
2015-03-18
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
40
Residue number B
52
Peptide name
R-spondin-2
Ligandability
Cysteine 40 of R-spondin-2
Cysteine 52 of R-spondin-2
4ufs B 110 B 113
A redox-regulated disulphide may form within R-spondin-2 between cysteines 110 and 113.
Details
Redox score ?
70
PDB code
4ufs
Structure name
low resolution structure r-spondin-2 (fu1fu2) in complex with the ectodomains of lgr5 and znrf3
Structure deposition date
2015-03-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
110
Residue number B
113
Peptide name
R-spondin-2
Ligandability
Cysteine 110 of R-spondin-2
Cysteine 113 of R-spondin-2
4ufr D 43 D 74
A redox-regulated disulphide may form within R-spondin-2 between cysteines 43 and 74.
Details
Redox score ?
70
PDB code
4ufr
Structure name
structure of the ectodomain of lgr5 in complex with r-spondin-2 (fu1fu2)
Structure deposition date
2015-03-18
Thiol separation (Å)
5
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
43
Residue number B
74
Peptide name
R-spondin-2
Ligandability
Cysteine 43 of R-spondin-2
Cysteine 74 of R-spondin-2
4c99 B 96 B 110
A redox-regulated disulphide may form within R-spondin-2 between cysteines 96 and 110.
Details
Redox score ?
70
PDB code
4c99
Structure name
mouse znrf3 ectodomain in complex with mouse rspo2 fu1-fu2 crystal form i
Structure deposition date
2013-10-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
96
Residue number B
110
Peptide name
R-spondin-2
Ligandability
Cysteine 96 of R-spondin-2
Cysteine 110 of R-spondin-2
4c99 B 101 B 113
A redox-regulated disulphide may form within R-spondin-2 between cysteines 101 and 113.
Details
Redox score ?
70
PDB code
4c99
Structure name
mouse znrf3 ectodomain in complex with mouse rspo2 fu1-fu2 crystal form i
Structure deposition date
2013-10-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
101
Residue number B
113
Peptide name
R-spondin-2
Ligandability
Cysteine 101 of R-spondin-2
Cysteine 113 of R-spondin-2
4ufs B 46 B 52
A redox-regulated disulphide may form within R-spondin-2 between cysteines 46 and 52.
Details
Redox score ?
67
PDB code
4ufs
Structure name
low resolution structure r-spondin-2 (fu1fu2) in complex with the ectodomains of lgr5 and znrf3
Structure deposition date
2015-03-18
Thiol separation (Å)
5
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
46
Residue number B
52
Peptide name
R-spondin-2
Ligandability
Cysteine 46 of R-spondin-2
Cysteine 52 of R-spondin-2
4ufr D 43 D 55
A redox-regulated disulphide may form within R-spondin-2 between cysteines 43 and 55.
Details
Redox score ?
64
PDB code
4ufr
Structure name
structure of the ectodomain of lgr5 in complex with r-spondin-2 (fu1fu2)
Structure deposition date
2015-03-18
Thiol separation (Å)
6
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
43
Residue number B
55
Peptide name
R-spondin-2
Ligandability
Cysteine 43 of R-spondin-2
Cysteine 55 of R-spondin-2
4ufr D 40 D 74
A redox-regulated disulphide may form within R-spondin-2 between cysteines 40 and 74. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
4ufr
Structure name
structure of the ectodomain of lgr5 in complex with r-spondin-2 (fu1fu2)
Structure deposition date
2015-03-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
40
Residue number B
74
Peptide name
R-spondin-2
Ligandability
Cysteine 40 of R-spondin-2
Cysteine 74 of R-spondin-2
4ufr B 40 B 55
A redox-regulated disulphide may form within R-spondin-2 between cysteines 40 and 55. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
4ufr
Structure name
structure of the ectodomain of lgr5 in complex with r-spondin-2 (fu1fu2)
Structure deposition date
2015-03-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
40
Residue number B
55
Peptide name
R-spondin-2
Ligandability
Cysteine 40 of R-spondin-2
Cysteine 55 of R-spondin-2
4ufr D 113 D 141
A redox-regulated disulphide may form within R-spondin-2 between cysteines 113 and 141. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
4ufr
Structure name
structure of the ectodomain of lgr5 in complex with r-spondin-2 (fu1fu2)
Structure deposition date
2015-03-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
113
Residue number B
141
Peptide name
R-spondin-2
Ligandability
Cysteine 113 of R-spondin-2
Cysteine 141 of R-spondin-2
4c99 B 78 B 96
A redox-regulated disulphide may form within R-spondin-2 between cysteines 78 and 96. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
4c99
Structure name
mouse znrf3 ectodomain in complex with mouse rspo2 fu1-fu2 crystal form i
Structure deposition date
2013-10-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
78
Residue number B
96
Peptide name
R-spondin-2
Ligandability
Cysteine 78 of R-spondin-2
Cysteine 96 of R-spondin-2
4c99 D 113 D 128
A redox-regulated disulphide may form within R-spondin-2 between cysteines 113 and 128. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
4c99
Structure name
mouse znrf3 ectodomain in complex with mouse rspo2 fu1-fu2 crystal form i
Structure deposition date
2013-10-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
113
Residue number B
128
Peptide name
R-spondin-2
Ligandability
Cysteine 113 of R-spondin-2
Cysteine 128 of R-spondin-2
4c99 D 55 D 78
A redox-regulated disulphide may form within R-spondin-2 between cysteines 55 and 78. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
4c99
Structure name
mouse znrf3 ectodomain in complex with mouse rspo2 fu1-fu2 crystal form i
Structure deposition date
2013-10-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
55
Residue number B
78
Peptide name
R-spondin-2
Ligandability
Cysteine 55 of R-spondin-2
Cysteine 78 of R-spondin-2
4ufr B 55 B 93
A redox-regulated disulphide may form within R-spondin-2 between cysteines 55 and 93. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
4ufr
Structure name
structure of the ectodomain of lgr5 in complex with r-spondin-2 (fu1fu2)
Structure deposition date
2015-03-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
55
Residue number B
93
Peptide name
R-spondin-2
Ligandability
Cysteine 55 of R-spondin-2
Cysteine 93 of R-spondin-2
4ufs B 46 B 74
A redox-regulated disulphide may form within R-spondin-2 between cysteines 46 and 74. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
4ufs
Structure name
low resolution structure r-spondin-2 (fu1fu2) in complex with the ectodomains of lgr5 and znrf3
Structure deposition date
2015-03-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
46
Residue number B
74
Peptide name
R-spondin-2
Ligandability
Cysteine 46 of R-spondin-2
Cysteine 74 of R-spondin-2
4c99 D 104 D 124
A redox-regulated disulphide may form within R-spondin-2 between cysteines 104 and 124. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
4c99
Structure name
mouse znrf3 ectodomain in complex with mouse rspo2 fu1-fu2 crystal form i
Structure deposition date
2013-10-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
104
Residue number B
124
Peptide name
R-spondin-2
Ligandability
Cysteine 104 of R-spondin-2
Cysteine 124 of R-spondin-2
4ufs B 78 B 104
A redox-regulated disulphide may form within R-spondin-2 between cysteines 78 and 104. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
4ufs
Structure name
low resolution structure r-spondin-2 (fu1fu2) in complex with the ectodomains of lgr5 and znrf3
Structure deposition date
2015-03-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
78
Residue number B
104
Peptide name
R-spondin-2
Ligandability
Cysteine 78 of R-spondin-2
Cysteine 104 of R-spondin-2
4c99 B 74 B 93
A redox-regulated disulphide may form within R-spondin-2 between cysteines 74 and 93. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
4c99
Structure name
mouse znrf3 ectodomain in complex with mouse rspo2 fu1-fu2 crystal form i
Structure deposition date
2013-10-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
74
Residue number B
93
Peptide name
R-spondin-2
Ligandability
Cysteine 74 of R-spondin-2
Cysteine 93 of R-spondin-2
4ufr B 124 B 141
A redox-regulated disulphide may form within R-spondin-2 between cysteines 124 and 141. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
4ufr
Structure name
structure of the ectodomain of lgr5 in complex with r-spondin-2 (fu1fu2)
Structure deposition date
2015-03-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
124
Residue number B
141
Peptide name
R-spondin-2
Ligandability
Cysteine 124 of R-spondin-2
Cysteine 141 of R-spondin-2
4c99 D 93 D 96
A redox-regulated disulphide may form within R-spondin-2 between cysteines 93 and 96. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
4c99
Structure name
mouse znrf3 ectodomain in complex with mouse rspo2 fu1-fu2 crystal form i
Structure deposition date
2013-10-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
93
Residue number B
96
Peptide name
R-spondin-2
Ligandability
Cysteine 93 of R-spondin-2
Cysteine 96 of R-spondin-2
4ufr D 96 D 124
A redox-regulated disulphide may form within R-spondin-2 between cysteines 96 and 124. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
4ufr
Structure name
structure of the ectodomain of lgr5 in complex with r-spondin-2 (fu1fu2)
Structure deposition date
2015-03-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BFU0
Residue number A
96
Residue number B
124
Peptide name
R-spondin-2
Ligandability
Cysteine 96 of R-spondin-2
Cysteine 124 of R-spondin-2
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