Cysteine-rich secretory protein 2
Intramolecular
Cysteine 189 and cysteine 196
Cysteine 192 and cysteine 201
Cysteine 205 and cysteine 238
Cysteine 214 and cysteine 232
Cysteine 223 and cysteine 236
Cysteine 192 and cysteine 196
Cysteine 189 and cysteine 192
Cysteine 196 and cysteine 201
Cysteine 223 and cysteine 232
Cysteine 189 and cysteine 201
More...Cysteine 232 and cysteine 236
Cysteine 214 and cysteine 223
Cysteine 214 and cysteine 236
Cysteine 201 and cysteine 205
Cysteine 223 and cysteine 238
Cysteine 205 and cysteine 214
Cysteine 201 and cysteine 238
Cysteine 192 and cysteine 205
Cysteine 214 and cysteine 238
Cysteine 232 and cysteine 238
Cysteine 236 and cysteine 238
2a05 A 189 A 196
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 189 and 196.
Details
Redox score ?
90
PDB code
2a05
Structure name
the cysteine-rich secretory protein domain of tpx-1 is related to ion channel toxins and regulates ryanodine receptor ca2+ signaling
Structure deposition date
2005-06-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
33
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16563
Residue number A
189
Residue number B
196
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 189 of Cysteine-rich secretory protein 2
Cysteine 196 of Cysteine-rich secretory protein 2
2a05 A 192 A 201
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 192 and 201.
Details
Redox score ?
88
PDB code
2a05
Structure name
the cysteine-rich secretory protein domain of tpx-1 is related to ion channel toxins and regulates ryanodine receptor ca2+ signaling
Structure deposition date
2005-06-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
36
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16563
Residue number A
192
Residue number B
201
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 192 of Cysteine-rich secretory protein 2
Cysteine 201 of Cysteine-rich secretory protein 2
2a05 A 205 A 238
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 205 and 238.
Details
Redox score ?
87
PDB code
2a05
Structure name
the cysteine-rich secretory protein domain of tpx-1 is related to ion channel toxins and regulates ryanodine receptor ca2+ signaling
Structure deposition date
2005-06-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16563
Residue number A
205
Residue number B
238
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 205 of Cysteine-rich secretory protein 2
Cysteine 238 of Cysteine-rich secretory protein 2
2cq7 A 18 A 36
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 214 and 232 (18 and 36 respectively in this structure).
Details
Redox score ?
86
PDB code
2cq7
Structure name
solution structure of rsgi ruh-032, a cystein-rich domain of crisp-2 from human cdna
Structure deposition date
2005-05-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16562
Residue number A
214
Residue number B
232
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 214 of Cysteine-rich secretory protein 2
Cysteine 232 of Cysteine-rich secretory protein 2
2cq7 A 27 A 40
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 223 and 236 (27 and 40 respectively in this structure).
Details
Redox score ?
85
PDB code
2cq7
Structure name
solution structure of rsgi ruh-032, a cystein-rich domain of crisp-2 from human cdna
Structure deposition date
2005-05-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16562
Residue number A
223
Residue number B
236
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 223 of Cysteine-rich secretory protein 2
Cysteine 236 of Cysteine-rich secretory protein 2
2a05 A 192 A 196
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 192 and 196.
Details
Redox score ?
76
PDB code
2a05
Structure name
the cysteine-rich secretory protein domain of tpx-1 is related to ion channel toxins and regulates ryanodine receptor ca2+ signaling
Structure deposition date
2005-06-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
34
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16563
Residue number A
192
Residue number B
196
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 192 of Cysteine-rich secretory protein 2
Cysteine 196 of Cysteine-rich secretory protein 2
2a05 A 189 A 192
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 189 and 192.
Details
Redox score ?
70
PDB code
2a05
Structure name
the cysteine-rich secretory protein domain of tpx-1 is related to ion channel toxins and regulates ryanodine receptor ca2+ signaling
Structure deposition date
2005-06-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
33
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16563
Residue number A
189
Residue number B
192
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 189 of Cysteine-rich secretory protein 2
Cysteine 192 of Cysteine-rich secretory protein 2
2a05 A 196 A 201
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 196 and 201.
Details
Redox score ?
68
PDB code
2a05
Structure name
the cysteine-rich secretory protein domain of tpx-1 is related to ion channel toxins and regulates ryanodine receptor ca2+ signaling
Structure deposition date
2005-06-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
36
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16563
Residue number A
196
Residue number B
201
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 196 of Cysteine-rich secretory protein 2
Cysteine 201 of Cysteine-rich secretory protein 2
2cq7 A 27 A 36
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 223 and 232 (27 and 36 respectively in this structure).
Details
Redox score ?
62
PDB code
2cq7
Structure name
solution structure of rsgi ruh-032, a cystein-rich domain of crisp-2 from human cdna
Structure deposition date
2005-05-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16562
Residue number A
223
Residue number B
232
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 223 of Cysteine-rich secretory protein 2
Cysteine 232 of Cysteine-rich secretory protein 2
2a05 A 189 A 201
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 189 and 201.
Details
Redox score ?
61
PDB code
2a05
Structure name
the cysteine-rich secretory protein domain of tpx-1 is related to ion channel toxins and regulates ryanodine receptor ca2+ signaling
Structure deposition date
2005-06-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
35
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16563
Residue number A
189
Residue number B
201
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 189 of Cysteine-rich secretory protein 2
Cysteine 201 of Cysteine-rich secretory protein 2
2cq7 A 36 A 40
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 232 and 236 (36 and 40 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
60
PDB code
2cq7
Structure name
solution structure of rsgi ruh-032, a cystein-rich domain of crisp-2 from human cdna
Structure deposition date
2005-05-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16562
Residue number A
232
Residue number B
236
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 232 of Cysteine-rich secretory protein 2
Cysteine 236 of Cysteine-rich secretory protein 2
2cq7 A 18 A 27
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 214 and 223 (18 and 27 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
2cq7
Structure name
solution structure of rsgi ruh-032, a cystein-rich domain of crisp-2 from human cdna
Structure deposition date
2005-05-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16562
Residue number A
214
Residue number B
223
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 214 of Cysteine-rich secretory protein 2
Cysteine 223 of Cysteine-rich secretory protein 2
2cq7 A 18 A 40
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 214 and 236 (18 and 40 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
2cq7
Structure name
solution structure of rsgi ruh-032, a cystein-rich domain of crisp-2 from human cdna
Structure deposition date
2005-05-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16562
Residue number A
214
Residue number B
236
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 214 of Cysteine-rich secretory protein 2
Cysteine 236 of Cysteine-rich secretory protein 2
2a05 A 201 A 205
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 201 and 205. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
2a05
Structure name
the cysteine-rich secretory protein domain of tpx-1 is related to ion channel toxins and regulates ryanodine receptor ca2+ signaling
Structure deposition date
2005-06-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
37
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16563
Residue number A
201
Residue number B
205
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 201 of Cysteine-rich secretory protein 2
Cysteine 205 of Cysteine-rich secretory protein 2
2cq7 A 27 A 42
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 223 and 238 (27 and 42 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
2cq7
Structure name
solution structure of rsgi ruh-032, a cystein-rich domain of crisp-2 from human cdna
Structure deposition date
2005-05-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16562
Residue number A
223
Residue number B
238
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 223 of Cysteine-rich secretory protein 2
Cysteine 238 of Cysteine-rich secretory protein 2
2a05 A 205 A 214
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 205 and 214. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
2a05
Structure name
the cysteine-rich secretory protein domain of tpx-1 is related to ion channel toxins and regulates ryanodine receptor ca2+ signaling
Structure deposition date
2005-06-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16563
Residue number A
205
Residue number B
214
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 205 of Cysteine-rich secretory protein 2
Cysteine 214 of Cysteine-rich secretory protein 2
2a05 A 201 A 238
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 201 and 238. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
2a05
Structure name
the cysteine-rich secretory protein domain of tpx-1 is related to ion channel toxins and regulates ryanodine receptor ca2+ signaling
Structure deposition date
2005-06-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16563
Residue number A
201
Residue number B
238
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 201 of Cysteine-rich secretory protein 2
Cysteine 238 of Cysteine-rich secretory protein 2
2a05 A 192 A 205
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 192 and 205. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
2a05
Structure name
the cysteine-rich secretory protein domain of tpx-1 is related to ion channel toxins and regulates ryanodine receptor ca2+ signaling
Structure deposition date
2005-06-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
35
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16563
Residue number A
192
Residue number B
205
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 192 of Cysteine-rich secretory protein 2
Cysteine 205 of Cysteine-rich secretory protein 2
2cq7 A 18 A 42
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 214 and 238 (18 and 42 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
2cq7
Structure name
solution structure of rsgi ruh-032, a cystein-rich domain of crisp-2 from human cdna
Structure deposition date
2005-05-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16562
Residue number A
214
Residue number B
238
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 214 of Cysteine-rich secretory protein 2
Cysteine 238 of Cysteine-rich secretory protein 2
2cq7 A 36 A 42
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 232 and 238 (36 and 42 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
2cq7
Structure name
solution structure of rsgi ruh-032, a cystein-rich domain of crisp-2 from human cdna
Structure deposition date
2005-05-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16562
Residue number A
232
Residue number B
238
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 232 of Cysteine-rich secretory protein 2
Cysteine 238 of Cysteine-rich secretory protein 2
2cq7 A 40 A 42
A redox-regulated disulphide may form within Cysteine-rich secretory protein 2 between cysteines 236 and 238 (40 and 42 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
2cq7
Structure name
solution structure of rsgi ruh-032, a cystein-rich domain of crisp-2 from human cdna
Structure deposition date
2005-05-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16562
Residue number A
236
Residue number B
238
Peptide name
Cysteine-rich secretory protein 2
Ligandability
Cysteine 236 of Cysteine-rich secretory protein 2
Cysteine 238 of Cysteine-rich secretory protein 2
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