ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Copper homeostasis protein cutC homolog

Intermolecular
Cysteine 248 and cysteine 248
Intramolecular
Cysteine 31 and cysteine 52
Cysteine 130 and cysteine 137
Cysteine 31 and cysteine 223
A redox-regulated disulphide may form between two units of Copper homeostasis protein cutC homolog at cysteines 248 and 248. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3iwp
Structure name
crystal structure of human copper homeostasis protein cutc
Structure deposition date
2009-09-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
32
Peptide A name
Copper homeostasis protein cutC homolog
Peptide B name
Copper homeostasis protein cutC homolog
Peptide A accession
Q9NTM9
Peptide B accession
Q9NTM9
Peptide A residue number
248
Peptide B residue number
248

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 Copper homeostasis protein cutC homolog between cysteines 31 and 52.

Details

Redox score ?
76
PDB code
3iwp
Structure name
crystal structure of human copper homeostasis protein cutc
Structure deposition date
2009-09-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NTM9
Residue number A
31
Residue number B
52
Peptide name
Copper homeostasis protein cutC homolog

Ligandability

Cysteine 31 of Copper homeostasis protein cutC homolog

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 52 of Copper homeostasis protein cutC homolog

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 Copper homeostasis protein cutC homolog between cysteines 130 and 137. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3iwp
Structure name
crystal structure of human copper homeostasis protein cutc
Structure deposition date
2009-09-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
84
Peptide accession
Q9NTM9
Residue number A
130
Residue number B
137
Peptide name
Copper homeostasis protein cutC homolog

Ligandability

Cysteine 130 of Copper homeostasis protein cutC homolog

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 137 of Copper homeostasis protein cutC homolog

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 Copper homeostasis protein cutC homolog between cysteines 31 and 223. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
3iwp
Structure name
crystal structure of human copper homeostasis protein cutc
Structure deposition date
2009-09-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
90
Minimum pKa ?
13
% buried
nan
Peptide accession
Q9NTM9
Residue number A
31
Residue number B
223
Peptide name
Copper homeostasis protein cutC homolog

Ligandability

Cysteine 31 of Copper homeostasis protein cutC homolog

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 223 of Copper homeostasis protein cutC homolog

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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