ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Copper chaperone for superoxide dismutase

Intramolecular
Cysteine 141 and cysteine 227 L
Cysteine 22 and cysteine 25
Cysteine 144 and cysteine 227 L
Cysteine 141 and cysteine 144
Cysteine 244 and cysteine 246 L
A redox-regulated disulphide may form within Copper chaperone for superoxide dismutase between cysteines 141 and 227.

Details

Redox score ?
85
PDB code
1do5
Structure name
human copper chaperone for superoxide dismutase domain ii
Structure deposition date
1999-12-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14618
Residue number A
141
Residue number B
227
Peptide name
Copper chaperone for superoxide dismutase

Ligandability

Cysteine 141 of Copper chaperone for superoxide dismutase

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 227 of Copper chaperone for superoxide dismutase

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Copper chaperone for superoxide dismutase between cysteines 22 and 25.

Details

Redox score ?
76
PDB code
2rsq
Structure name
copper(i) loaded form of the first domain of the human copper chaperone for sod1, ccs
Structure deposition date
2012-05-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
9
% buried
0
Peptide accession
O14618
Residue number A
22
Residue number B
25
Peptide name
Copper chaperone for superoxide dismutase

Ligandability

Cysteine 22 of Copper chaperone for superoxide dismutase

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 25 of Copper chaperone for superoxide dismutase

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 chaperone for superoxide dismutase between cysteines 144 and 227.

Details

Redox score ?
67
PDB code
6fp6
Structure name
complex of human cu,zn sod1 with the human copper chaperone for sod1 in a compact conformation
Structure deposition date
2018-02-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
11
% buried
nan
Peptide accession
O14618
Residue number A
144
Residue number B
227
Peptide name
Copper chaperone for superoxide dismutase

Ligandability

Cysteine 144 of Copper chaperone for superoxide dismutase

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 227 of Copper chaperone for superoxide dismutase

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Copper chaperone for superoxide dismutase between cysteines 141 and 144.

Details

Redox score ?
65
PDB code
6fol
Structure name
domain ii of the human copper chaperone in complex with human cu,zn superoxide dismutase
Structure deposition date
2018-02-07
Thiol separation (Å)
6
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
nan
Peptide accession
O14618
Residue number A
141
Residue number B
144
Peptide name
Copper chaperone for superoxide dismutase

Ligandability

Cysteine 141 of Copper chaperone for superoxide dismutase

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 144 of Copper chaperone for superoxide dismutase

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 chaperone for superoxide dismutase between cysteines 244 and 246.

Details

Redox score ?
61
PDB code
6fon
Structure name
elongated conformer of the human copper chaperone for sod1 complexed with human sod1
Structure deposition date
2018-02-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
37
Minimum pKa ?
9
% buried
0
Peptide accession
O14618
Residue number A
244
Residue number B
246
Peptide name
Copper chaperone for superoxide dismutase

Ligandability

Cysteine 244 of Copper chaperone for superoxide dismutase

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 246 of Copper chaperone for superoxide dismutase

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.

Ligandable in the dataset of Kuljanin et al.

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