ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Prostasin

Intermolecular
Cysteine 86 and cysteine 49 of Pancreatic trypsin inhibitor
Cysteine 70 and cysteine 49 of Pancreatic trypsin inhibitor
Intramolecular
Cysteine 168 and cysteine 244
Cysteine 201 and cysteine 223
Cysteine 234 and cysteine 262
Cysteine 70 and cysteine 86
A redox-regulated disulphide may form between cysteine 86 of Prostasin and cysteine 49 of Pancreatic trypsin inhibitor (58 and 14 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
3gym
Structure name
structure of prostasin in complex with aprotinin
Structure deposition date
2009-04-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide A name
Prostasin
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
Q16651
Peptide B accession
P00974
Peptide A residue number
86
Peptide B residue number
49

Ligandability

Cysteine 86 of Prostasin

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 49 of Pancreatic trypsin inhibitor

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 between cysteine 70 of Prostasin and cysteine 49 of Pancreatic trypsin inhibitor (42 and 14 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
3gym
Structure name
structure of prostasin in complex with aprotinin
Structure deposition date
2009-04-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide A name
Prostasin
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
Q16651
Peptide B accession
P00974
Peptide A residue number
70
Peptide B residue number
49

Ligandability

Cysteine 70 of Prostasin

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 49 of Pancreatic trypsin inhibitor

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 Prostasin between cysteines 168 and 244.

Details

Redox score ?
84
PDB code
3dfj
Structure name
crystal structure of human prostasin
Structure deposition date
2008-06-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16651
Residue number A
168
Residue number B
244
Peptide name
Prostasin

Ligandability

Cysteine 168 of Prostasin

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 244 of Prostasin

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 Prostasin between cysteines 201 and 223.

Details

Redox score ?
81
PDB code
3dfl
Structure name
crystal structure of human prostasin complexed to 4-guanidinobenzoic acid
Structure deposition date
2008-06-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16651
Residue number A
201
Residue number B
223
Peptide name
Prostasin

Ligandability

Cysteine 201 of Prostasin

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 223 of Prostasin

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 Prostasin between cysteines 234 and 262 (191 and 219 respectively in this structure).

Details

Redox score ?
80
PDB code
3e16
Structure name
x-ray structure of human prostasin in complex with benzoxazole warhead peptidomimic, lysine in p3
Structure deposition date
2008-08-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16651
Residue number A
234
Residue number B
262
Peptide name
Prostasin

Ligandability

Cysteine 234 of Prostasin

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 262 of Prostasin

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 Prostasin between cysteines 70 and 86 (42 and 58 respectively in this structure).

Details

Redox score ?
80
PDB code
3e0p
Structure name
the x-ray structure of human prostasin in complex with a covalent benzoxazole inhibitor
Structure deposition date
2008-07-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16651
Residue number A
70
Residue number B
86
Peptide name
Prostasin

Ligandability

Cysteine 70 of Prostasin

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 86 of Prostasin

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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