ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Pancreatic triacylglycerol lipase

Intramolecular
Cysteine 302 and cysteine 313
Cysteine 449 and cysteine 465
Cysteine 250 and cysteine 274
Cysteine 16 and cysteine 22
Cysteine 316 and cysteine 321
Cysteine 107 and cysteine 118
Cysteine 107 and cysteine 120
Cysteine 102 and cysteine 104
Cysteine 297 and cysteine 305
Cysteine 297 and cysteine 300
A redox-regulated disulphide may form within Pancreatic triacylglycerol lipase between cysteines 302 and 313 (285 and 296 respectively in this structure).

Details

Redox score ?
86
PDB code
1lpb
Structure name
the 2
Structure deposition date
1994-08-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16233
Residue number A
302
Residue number B
313
Peptide name
Pancreatic triacylglycerol lipase

Ligandability

Cysteine 302 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 313 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Pancreatic triacylglycerol lipase between cysteines 449 and 465 (433 and 449 respectively in this structure).

Details

Redox score ?
86
PDB code
1gpl
Structure name
rp2 lipase
Structure deposition date
1996-07-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16233
Residue number A
449
Residue number B
465
Peptide name
Pancreatic triacylglycerol lipase

Ligandability

Cysteine 449 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 465 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Pancreatic triacylglycerol lipase between cysteines 250 and 274 (237 and 261 respectively in this structure).

Details

Redox score ?
84
PDB code
1hpl
Structure name
horse pancreatic lipase
Structure deposition date
1993-01-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29183
Residue number A
250
Residue number B
274
Peptide name
Pancreatic triacylglycerol lipase

Ligandability

Cysteine 250 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 274 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Pancreatic triacylglycerol lipase between cysteines 16 and 22 (4 and 10 respectively in this structure).

Details

Redox score ?
84
PDB code
1hpl
Structure name
horse pancreatic lipase
Structure deposition date
1993-01-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
38
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29183
Residue number A
16
Residue number B
22
Peptide name
Pancreatic triacylglycerol lipase

Ligandability

Cysteine 16 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 22 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Pancreatic triacylglycerol lipase between cysteines 316 and 321 (299 and 304 respectively in this structure).

Details

Redox score ?
83
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 ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16233
Residue number A
316
Residue number B
321
Peptide name
Pancreatic triacylglycerol lipase

Ligandability

Cysteine 316 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 321 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Pancreatic triacylglycerol lipase between cysteines 107 and 118 (90 and 101 respectively in this structure).

Details

Redox score ?
80
PDB code
1lpb
Structure name
the 2
Structure deposition date
1994-08-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16233
Residue number A
107
Residue number B
118
Peptide name
Pancreatic triacylglycerol lipase

Ligandability

Cysteine 107 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 118 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Pancreatic triacylglycerol lipase between cysteines 107 and 120 (90 and 103 respectively in this structure).

Details

Redox score ?
62
PDB code
1lpb
Structure name
the 2
Structure deposition date
1994-08-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
nan
Peptide accession
P16233
Residue number A
107
Residue number B
120
Peptide name
Pancreatic triacylglycerol lipase

Ligandability

Cysteine 107 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 120 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Pancreatic triacylglycerol lipase between cysteines 102 and 104. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
1eth
Structure name
triacylglycerol lipase/colipase complex
Structure deposition date
1995-09-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
92
Minimum pKa ?
13
% buried
nan
Peptide accession
P00591
Residue number A
102
Residue number B
104
Peptide name
Pancreatic triacylglycerol lipase

Ligandability

Cysteine 102 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 104 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Pancreatic triacylglycerol lipase between cysteines 297 and 305. 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)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00591
Residue number A
297
Residue number B
305
Peptide name
Pancreatic triacylglycerol lipase

Ligandability

Cysteine 297 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 305 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Pancreatic triacylglycerol lipase between cysteines 297 and 300. 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)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00591
Residue number A
297
Residue number B
300
Peptide name
Pancreatic triacylglycerol lipase

Ligandability

Cysteine 297 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 300 of Pancreatic triacylglycerol lipase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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