ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Hepatopancreas trypsin

Intermolecular
Cysteine 46 and cysteine 49 of Pancreatic trypsin inhibitor
Cysteine 30 and cysteine 49 of Pancreatic trypsin inhibitor
A redox-regulated disulphide may form between cysteine 46 of Hepatopancreas trypsin 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 ?
40
PDB code
4bnr
Structure name
extremely stable complex of crayfish trypsin with bovine trypsin inhibitor
Structure deposition date
2013-05-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
97
Minimum pKa ?
nan
% buried
nan
Peptide A name
Hepatopancreas trypsin
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
Q52V24
Peptide B accession
P00974
Peptide A residue number
46
Peptide B residue number
49

Ligandability

Cysteine 46 of Hepatopancreas trypsin

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 30 of Hepatopancreas trypsin 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 ?
35
PDB code
4bnr
Structure name
extremely stable complex of crayfish trypsin with bovine trypsin inhibitor
Structure deposition date
2013-05-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide A name
Hepatopancreas trypsin
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
Q52V24
Peptide B accession
P00974
Peptide A residue number
30
Peptide B residue number
49

Ligandability

Cysteine 30 of Hepatopancreas trypsin

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.

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