ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Renin

Intramolecular
Cysteine 117 and cysteine 124
Cysteine 325 and cysteine 362
Cysteine 283 and cysteine 287
A redox-regulated disulphide may form within Renin between cysteines 117 and 124 (51 and 58 respectively in this structure).

Details

Redox score ?
87
PDB code
5sy2
Structure name
structure-based design of a new series of n-piperidin-3-ylpyrimidine- 5-carboxamides as renin inhibitors
Structure deposition date
2016-08-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00797
Residue number A
117
Residue number B
124
Peptide name
Renin

Ligandability

Cysteine 117 of Renin

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 124 of Renin

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 Renin between cysteines 325 and 362 (254 and 291 respectively in this structure).

Details

Redox score ?
85
PDB code
2g1s
Structure name
ketopiperazine-based renin inhibitors: optimization of the c ring
Structure deposition date
2006-02-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00797
Residue number A
325
Residue number B
362
Peptide name
Renin

Ligandability

Cysteine 325 of Renin

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 362 of Renin

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 Renin between cysteines 283 and 287 (217 and 221 respectively in this structure).

Details

Redox score ?
85
PDB code
7xgp
Structure name
human renin in complex with compound3
Structure deposition date
2022-04-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00797
Residue number A
283
Residue number B
287
Peptide name
Renin

Ligandability

Cysteine 283 of Renin

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 287 of Renin

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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