ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cytochrome c oxidase copper chaperone

Intramolecular
Cysteine 36 and cysteine 45
Cysteine 26 and cysteine 55
Cysteine 23 and cysteine 24
Cysteine 23 and cysteine 26
Cysteine 24 and cysteine 26
Cysteine 24 and cysteine 55
A redox-regulated disulphide may form within Cytochrome c oxidase copper chaperone between cysteines 36 and 45 (40 and 49 respectively in this structure).

Details

Redox score ?
87
PDB code
2rn9
Structure name
solution structure of human apocox17
Structure deposition date
2007-12-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q14061
Residue number A
36
Residue number B
45
Peptide name
Cytochrome c oxidase copper chaperone

Ligandability

Cysteine 36 of Cytochrome c oxidase copper chaperone

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 45 of Cytochrome c oxidase copper chaperone

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 Cytochrome c oxidase copper chaperone between cysteines 26 and 55 (30 and 59 respectively in this structure).

Details

Redox score ?
83
PDB code
2rnb
Structure name
solution structure of human cu(i)cox17
Structure deposition date
2007-12-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q14061
Residue number A
26
Residue number B
55
Peptide name
Cytochrome c oxidase copper chaperone

Ligandability

Cysteine 26 of Cytochrome c oxidase copper chaperone

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 55 of Cytochrome c oxidase copper chaperone

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 Cytochrome c oxidase copper chaperone between cysteines 23 and 24 (27 and 28 respectively in this structure).

Details

Redox score ?
78
PDB code
2rnb
Structure name
solution structure of human cu(i)cox17
Structure deposition date
2007-12-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
8
% buried
0
Peptide accession
Q14061
Residue number A
23
Residue number B
24
Peptide name
Cytochrome c oxidase copper chaperone

Ligandability

Cysteine 23 of Cytochrome c oxidase copper chaperone

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 24 of Cytochrome c oxidase copper chaperone

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 Cytochrome c oxidase copper chaperone between cysteines 23 and 26 (27 and 30 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
2rn9
Structure name
solution structure of human apocox17
Structure deposition date
2007-12-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
28
Minimum pKa ?
9
% buried
nan
Peptide accession
Q14061
Residue number A
23
Residue number B
26
Peptide name
Cytochrome c oxidase copper chaperone

Ligandability

Cysteine 23 of Cytochrome c oxidase copper chaperone

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 26 of Cytochrome c oxidase copper chaperone

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 Cytochrome c oxidase copper chaperone between cysteines 24 and 26 (28 and 30 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2rn9
Structure name
solution structure of human apocox17
Structure deposition date
2007-12-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
33
Minimum pKa ?
9
% buried
nan
Peptide accession
Q14061
Residue number A
24
Residue number B
26
Peptide name
Cytochrome c oxidase copper chaperone

Ligandability

Cysteine 24 of Cytochrome c oxidase copper chaperone

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 26 of Cytochrome c oxidase copper chaperone

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 Cytochrome c oxidase copper chaperone between cysteines 24 and 55 (28 and 59 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2rn9
Structure name
solution structure of human apocox17
Structure deposition date
2007-12-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
35
Minimum pKa ?
9
% buried
nan
Peptide accession
Q14061
Residue number A
24
Residue number B
55
Peptide name
Cytochrome c oxidase copper chaperone

Ligandability

Cysteine 24 of Cytochrome c oxidase copper chaperone

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 55 of Cytochrome c oxidase copper chaperone

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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