ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Protein NDRG3

Intermolecular
Cysteine 30 and cysteine 30
Intramolecular
Cysteine 166 and cysteine 273 L
Cysteine 30 and cysteine 90
A redox-regulated disulphide may form between two units of Protein NDRG3 at cysteines 30 and 30.

Details

Redox score ?
87
PDB code
6l4b
Structure name
crystal structure of human wt ndrg3
Structure deposition date
2019-10-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide A name
Protein NDRG3
Peptide B name
Protein NDRG3
Peptide A accession
Q9UGV2
Peptide B accession
Q9UGV2
Peptide A residue number
30
Peptide B residue number
30

Ligandability

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 Protein NDRG3 between cysteines 166 and 273. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6l4b
Structure name
crystal structure of human wt ndrg3
Structure deposition date
2019-10-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
64
Peptide accession
Q9UGV2
Residue number A
166
Residue number B
273
Peptide name
Protein NDRG3

Ligandability

Cysteine 166 of Protein NDRG3

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.

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 273 of Protein NDRG3

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 Protein NDRG3 between cysteines 30 and 90. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6l4g
Structure name
crystal structure of human ndrg3 i171m/s176h mutant
Structure deposition date
2019-10-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
12
% buried
nan
Peptide accession
Q9UGV2
Residue number A
30
Residue number B
90
Peptide name
Protein NDRG3

Ligandability

Cysteine 30 of Protein NDRG3

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 90 of Protein NDRG3

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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