Colipase
Intramolecular
Cysteine 80 and cysteine 104
Cysteine 66 and cysteine 86
Cysteine 34 and cysteine 45
Cysteine 40 and cysteine 56
Cysteine 44 and cysteine 78
Cysteine 34 and cysteine 40
Cysteine 66 and cysteine 80
Cysteine 80 and cysteine 86
Cysteine 34 and cysteine 56
Cysteine 40 and cysteine 45
More...Cysteine 86 and cysteine 104
Cysteine 66 and cysteine 104
Cysteine 45 and cysteine 56
Cysteine 40 and cysteine 44
Cysteine 34 and cysteine 44
Cysteine 44 and cysteine 45
Cysteine 40 and cysteine 78
Cysteine 44 and cysteine 56
Cysteine 34 and cysteine 78
Cysteine 45 and cysteine 78
Cysteine 78 and cysteine 80
Cysteine 78 and cysteine 86
Cysteine 56 and cysteine 78
Cysteine 78 and cysteine 104
Cysteine 44 and cysteine 66
Cysteine 66 and cysteine 78
Cysteine 44 and cysteine 86
1eth B 63 B 87
A redox-regulated disulphide may form within Colipase between cysteines 80 and 104 (63 and 87 respectively in this structure).
Details
Redox score ?
86
PDB code
1eth
Structure name
triacylglycerol lipase/colipase complex
Structure deposition date
1995-09-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
80
Residue number B
104
Peptide name
Colipase
Ligandability
Cysteine 80 of Colipase
Cysteine 104 of Colipase
1n8s C 549 C 569
A redox-regulated disulphide may form within Colipase between cysteines 66 and 86 (549 and 569 respectively in this structure).
Details
Redox score ?
85
PDB code
1n8s
Structure name
structure of the pancreatic lipase-colipase complex
Structure deposition date
2002-11-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
66
Residue number B
86
Peptide name
Colipase
Ligandability
Cysteine 66 of Colipase
Cysteine 86 of Colipase
1lpa A 17 A 28
A redox-regulated disulphide may form within Colipase between cysteines 34 and 45 (17 and 28 respectively in this structure).
Details
Redox score ?
85
PDB code
1lpa
Structure name
interfacial activation of the lipase-procolipase complex by mixed micelles revealed by x-ray crystallography
Structure deposition date
1994-08-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
34
Residue number B
45
Peptide name
Colipase
Ligandability
Cysteine 34 of Colipase
Cysteine 45 of Colipase
1eth D 23 D 39
A redox-regulated disulphide may form within Colipase between cysteines 40 and 56 (23 and 39 respectively in this structure).
Details
Redox score ?
85
PDB code
1eth
Structure name
triacylglycerol lipase/colipase complex
Structure deposition date
1995-09-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
40
Residue number B
56
Peptide name
Colipase
Ligandability
Cysteine 40 of Colipase
Cysteine 56 of Colipase
1n8s C 527 C 561
A redox-regulated disulphide may form within Colipase between cysteines 44 and 78 (527 and 561 respectively in this structure).
Details
Redox score ?
78
PDB code
1n8s
Structure name
structure of the pancreatic lipase-colipase complex
Structure deposition date
2002-11-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
44
Residue number B
78
Peptide name
Colipase
Ligandability
Cysteine 44 of Colipase
Cysteine 78 of Colipase
1eth B 17 B 23
A redox-regulated disulphide may form within Colipase between cysteines 34 and 40 (17 and 23 respectively in this structure).
Details
Redox score ?
78
PDB code
1eth
Structure name
triacylglycerol lipase/colipase complex
Structure deposition date
1995-09-13
Thiol separation (Å)
3
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
34
Residue number B
40
Peptide name
Colipase
Ligandability
Cysteine 34 of Colipase
Cysteine 40 of Colipase
1eth D 49 D 63
A redox-regulated disulphide may form within Colipase between cysteines 66 and 80 (49 and 63 respectively in this structure).
Details
Redox score ?
77
PDB code
1eth
Structure name
triacylglycerol lipase/colipase complex
Structure deposition date
1995-09-13
Thiol separation (Å)
3
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
66
Residue number B
80
Peptide name
Colipase
Ligandability
Cysteine 66 of Colipase
Cysteine 80 of Colipase
1n8s C 563 C 569
A redox-regulated disulphide may form within Colipase between cysteines 80 and 86 (563 and 569 respectively in this structure).
Details
Redox score ?
77
PDB code
1n8s
Structure name
structure of the pancreatic lipase-colipase complex
Structure deposition date
2002-11-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
80
Residue number B
86
Peptide name
Colipase
Ligandability
Cysteine 80 of Colipase
Cysteine 86 of Colipase
1lpb A 17 A 39
A redox-regulated disulphide may form within Colipase between cysteines 34 and 56 (17 and 39 respectively in this structure).
Details
Redox score ?
74
PDB code
1lpb
Structure name
the 2
Structure deposition date
1994-08-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
34
Residue number B
56
Peptide name
Colipase
Ligandability
Cysteine 34 of Colipase
Cysteine 56 of Colipase
1n8s C 523 C 528
A redox-regulated disulphide may form within Colipase between cysteines 40 and 45 (523 and 528 respectively in this structure).
Details
Redox score ?
70
PDB code
1n8s
Structure name
structure of the pancreatic lipase-colipase complex
Structure deposition date
2002-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
40
Residue number B
45
Peptide name
Colipase
Ligandability
Cysteine 40 of Colipase
Cysteine 45 of Colipase
1eth B 69 B 87
A redox-regulated disulphide may form within Colipase between cysteines 86 and 104 (69 and 87 respectively in this structure).
Details
Redox score ?
70
PDB code
1eth
Structure name
triacylglycerol lipase/colipase complex
Structure deposition date
1995-09-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
86
Residue number B
104
Peptide name
Colipase
Ligandability
Cysteine 86 of Colipase
Cysteine 104 of Colipase
1n8s C 549 C 587
A redox-regulated disulphide may form within Colipase between cysteines 66 and 104 (549 and 587 respectively in this structure).
Details
Redox score ?
68
PDB code
1n8s
Structure name
structure of the pancreatic lipase-colipase complex
Structure deposition date
2002-11-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
66
Residue number B
104
Peptide name
Colipase
Ligandability
Cysteine 66 of Colipase
Cysteine 104 of Colipase
1n8s C 528 C 539
A redox-regulated disulphide may form within Colipase between cysteines 45 and 56 (528 and 539 respectively in this structure).
Details
Redox score ?
60
PDB code
1n8s
Structure name
structure of the pancreatic lipase-colipase complex
Structure deposition date
2002-11-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
45
Residue number B
56
Peptide name
Colipase
Ligandability
Cysteine 45 of Colipase
Cysteine 56 of Colipase
1eth B 23 B 27
A redox-regulated disulphide may form within Colipase between cysteines 40 and 44 (23 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 ?
55
PDB code
1eth
Structure name
triacylglycerol lipase/colipase complex
Structure deposition date
1995-09-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
40
Residue number B
44
Peptide name
Colipase
Ligandability
Cysteine 40 of Colipase
Cysteine 44 of Colipase
1lpa A 17 A 27
A redox-regulated disulphide may form within Colipase between cysteines 34 and 44 (17 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 ?
51
PDB code
1lpa
Structure name
interfacial activation of the lipase-procolipase complex by mixed micelles revealed by x-ray crystallography
Structure deposition date
1994-08-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
34
Residue number B
44
Peptide name
Colipase
Ligandability
Cysteine 34 of Colipase
Cysteine 44 of Colipase
1eth B 27 B 28
A redox-regulated disulphide may form within Colipase between cysteines 44 and 45 (27 and 28 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
1eth
Structure name
triacylglycerol lipase/colipase complex
Structure deposition date
1995-09-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
44
Residue number B
45
Peptide name
Colipase
Ligandability
Cysteine 44 of Colipase
Cysteine 45 of Colipase
1lpb A 23 A 61
A redox-regulated disulphide may form within Colipase between cysteines 40 and 78 (23 and 61 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
1lpb
Structure name
the 2
Structure deposition date
1994-08-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
40
Residue number B
78
Peptide name
Colipase
Ligandability
Cysteine 40 of Colipase
Cysteine 78 of Colipase
1eth D 27 D 39
A redox-regulated disulphide may form within Colipase between cysteines 44 and 56 (27 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 ?
44
PDB code
1eth
Structure name
triacylglycerol lipase/colipase complex
Structure deposition date
1995-09-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
44
Residue number B
56
Peptide name
Colipase
Ligandability
Cysteine 44 of Colipase
Cysteine 56 of Colipase
1lpa A 17 A 61
A redox-regulated disulphide may form within Colipase between cysteines 34 and 78 (17 and 61 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
1lpa
Structure name
interfacial activation of the lipase-procolipase complex by mixed micelles revealed by x-ray crystallography
Structure deposition date
1994-08-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
34
Residue number B
78
Peptide name
Colipase
Ligandability
Cysteine 34 of Colipase
Cysteine 78 of Colipase
1eth B 28 B 61
A redox-regulated disulphide may form within Colipase between cysteines 45 and 78 (28 and 61 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
1eth
Structure name
triacylglycerol lipase/colipase complex
Structure deposition date
1995-09-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
45
Residue number B
78
Peptide name
Colipase
Ligandability
Cysteine 45 of Colipase
Cysteine 78 of Colipase
1eth D 61 D 63
A redox-regulated disulphide may form within Colipase between cysteines 78 and 80 (61 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
1eth
Structure name
triacylglycerol lipase/colipase complex
Structure deposition date
1995-09-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
78
Residue number B
80
Peptide name
Colipase
Ligandability
Cysteine 78 of Colipase
Cysteine 80 of Colipase
1pco A 61 A 69
A redox-regulated disulphide may form within Colipase between cysteines 78 and 86 (61 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 ?
39
PDB code
1pco
Structure name
solution structure of porcine pancreatic procolipase as determined from 1h homonuclear two-and three-dimensional nmr
Structure deposition date
1994-06-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
78
Residue number B
86
Peptide name
Colipase
Ligandability
Cysteine 78 of Colipase
Cysteine 86 of Colipase
1n8s C 539 C 561
A redox-regulated disulphide may form within Colipase between cysteines 56 and 78 (539 and 561 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
1n8s
Structure name
structure of the pancreatic lipase-colipase complex
Structure deposition date
2002-11-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
56
Residue number B
78
Peptide name
Colipase
Ligandability
Cysteine 56 of Colipase
Cysteine 78 of Colipase
1lpa A 61 A 87
A redox-regulated disulphide may form within Colipase between cysteines 78 and 104 (61 and 87 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
1lpa
Structure name
interfacial activation of the lipase-procolipase complex by mixed micelles revealed by x-ray crystallography
Structure deposition date
1994-08-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
78
Residue number B
104
Peptide name
Colipase
Ligandability
Cysteine 78 of Colipase
Cysteine 104 of Colipase
1pco A 27 A 49
A redox-regulated disulphide may form within Colipase between cysteines 44 and 66 (27 and 49 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
1pco
Structure name
solution structure of porcine pancreatic procolipase as determined from 1h homonuclear two-and three-dimensional nmr
Structure deposition date
1994-06-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
44
Residue number B
66
Peptide name
Colipase
Ligandability
Cysteine 44 of Colipase
Cysteine 66 of Colipase
1lpa A 49 A 61
A redox-regulated disulphide may form within Colipase between cysteines 66 and 78 (49 and 61 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
1lpa
Structure name
interfacial activation of the lipase-procolipase complex by mixed micelles revealed by x-ray crystallography
Structure deposition date
1994-08-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
66
Residue number B
78
Peptide name
Colipase
Ligandability
Cysteine 66 of Colipase
Cysteine 78 of Colipase
1pco A 27 A 69
A redox-regulated disulphide may form within Colipase between cysteines 44 and 86 (27 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
1pco
Structure name
solution structure of porcine pancreatic procolipase as determined from 1h homonuclear two-and three-dimensional nmr
Structure deposition date
1994-06-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02703
Residue number A
44
Residue number B
86
Peptide name
Colipase
Ligandability
Cysteine 44 of Colipase
Cysteine 86 of Colipase
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