ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Renalase

Intramolecular
Cysteine 65 and cysteine 103
Cysteine 47 and cysteine 54
Cysteine 16 and cysteine 333
Cysteine 16 and cysteine 327
A redox-regulated disulphide may form within Renalase between cysteines 65 and 103. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
3qj4
Structure name
crystal structure of human renalase (isoform 1)
Structure deposition date
2011-01-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
24
Peptide accession
Q5VYX0
Residue number A
65
Residue number B
103
Peptide name
Renalase

Ligandability

Cysteine 65 of Renalase

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 103 of Renalase

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 Renalase between cysteines 47 and 54. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3qj4
Structure name
crystal structure of human renalase (isoform 1)
Structure deposition date
2011-01-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
24
Peptide accession
Q5VYX0
Residue number A
47
Residue number B
54
Peptide name
Renalase

Ligandability

Cysteine 47 of Renalase

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 54 of Renalase

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 Renalase between cysteines 16 and 333. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
3qj4
Structure name
crystal structure of human renalase (isoform 1)
Structure deposition date
2011-01-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
10
% buried
66
Peptide accession
Q5VYX0
Residue number A
16
Residue number B
333
Peptide name
Renalase

Ligandability

Cysteine 16 of Renalase

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 Renalase

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 Renalase between cysteines 16 and 327. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
3qj4
Structure name
crystal structure of human renalase (isoform 1)
Structure deposition date
2011-01-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
100
Peptide accession
Q5VYX0
Residue number A
16
Residue number B
327
Peptide name
Renalase

Ligandability

Cysteine 16 of Renalase

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 327 of Renalase

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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