ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Furin

Intramolecular
Cysteine 211 and cysteine 360
Cysteine 450 and cysteine 474
Cysteine 303 and cysteine 333
Cysteine 305 and cysteine 333
Cysteine 303 and cysteine 305
A redox-regulated disulphide may form within Furin between cysteines 211 and 360.

Details

Redox score ?
82
PDB code
1p8j
Structure name
crystal structure of the proprotein convertase furin
Structure deposition date
2003-05-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P23188
Residue number A
211
Residue number B
360
Peptide name
Furin

Ligandability

Cysteine 211 of Furin

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 360 of Furin

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 Furin between cysteines 450 and 474.

Details

Redox score ?
81
PDB code
4omd
Structure name
x-ray structure of human furin in complex with the competitive inhibitor phac-rvr-amba
Structure deposition date
2014-01-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09958
Residue number A
450
Residue number B
474
Peptide name
Furin

Ligandability

Cysteine 450 of Furin

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 474 of Furin

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 Furin between cysteines 303 and 333.

Details

Redox score ?
78
PDB code
4omc
Structure name
x-ray structure of human furin in complex with the competitive inhibitor meta-guanidinomethyl-phac-rvr-amba
Structure deposition date
2014-01-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
101
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09958
Residue number A
303
Residue number B
333
Peptide name
Furin

Ligandability

Cysteine 303 of Furin

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 333 of Furin

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 Furin between cysteines 305 and 333. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6hld
Structure name
x-ray structure of furin in complex with the cyclic peptide c[succinyl-phe-2-nal-(arg)3-lys]-lys-4-amba
Structure deposition date
2018-09-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
91
Minimum pKa ?
11
% buried
nan
Peptide accession
P09958
Residue number A
305
Residue number B
333
Peptide name
Furin

Ligandability

Cysteine 305 of Furin

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 333 of Furin

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 Furin between cysteines 303 and 305. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
7qxz
Structure name
x-ray structure of furin in complex with the dichlorophenylpyridine- based inhibitor 5
Structure deposition date
2022-01-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
99
Minimum pKa ?
11
% buried
nan
Peptide accession
P09958
Residue number A
303
Residue number B
305
Peptide name
Furin

Ligandability

Cysteine 303 of Furin

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 Furin

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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