ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Copper-transporting ATPase 2

Intramolecular
Cysteine 69 and cysteine 72
Cysteine 575 and cysteine 578
Cysteine 154 and cysteine 157 L
Cysteine 370 and cysteine 373
Cysteine 1091 and cysteine 1104
Cysteine 268 and cysteine 271
Cysteine 499 and cysteine 502 L
Cysteine 108 and cysteine 113
Cysteine 1104 and cysteine 1189
A redox-regulated disulphide may form within Copper-transporting ATPase 2 between cysteines 69 and 72 (18 and 21 respectively in this structure).

Details

Redox score ?
75
PDB code
2n7y
Structure name
nmr structure of metal-binding domain 1 of atp7b
Structure deposition date
2015-09-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
7
Peptide accession
P35670
Residue number A
69
Residue number B
72
Peptide name
Copper-transporting ATPase 2

Ligandability

Cysteine 69 of Copper-transporting ATPase 2

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 72 of Copper-transporting ATPase 2

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-transporting ATPase 2 between cysteines 575 and 578 (91 and 94 respectively in this structure).

Details

Redox score ?
72
PDB code
2ew9
Structure name
solution structure of apowln5-6
Structure deposition date
2005-11-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
37
Minimum pKa ?
8
% buried
0
Peptide accession
P35670
Residue number A
575
Residue number B
578
Peptide name
Copper-transporting ATPase 2

Ligandability

Cysteine 575 of Copper-transporting ATPase 2

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 578 of Copper-transporting ATPase 2

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-transporting ATPase 2 between cysteines 154 and 157 (18 and 21 respectively in this structure).

Details

Redox score ?
70
PDB code
2lqb
Structure name
metal binding repeat 2 of the wilson disease protein (atp7b)
Structure deposition date
2012-02-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
32
Minimum pKa ?
9
% buried
0
Peptide accession
P35670
Residue number A
154
Residue number B
157
Peptide name
Copper-transporting ATPase 2

Ligandability

Cysteine 154 of Copper-transporting ATPase 2

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 157 of Copper-transporting ATPase 2

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-transporting ATPase 2 between cysteines 370 and 373 (133 and 136 respectively in this structure).

Details

Redox score ?
66
PDB code
2rop
Structure name
solution structure of domains 3 and 4 of human atp7b
Structure deposition date
2008-04-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
41
Minimum pKa ?
9
% buried
0
Peptide accession
P35670
Residue number A
370
Residue number B
373
Peptide name
Copper-transporting ATPase 2

Ligandability

Cysteine 370 of Copper-transporting ATPase 2

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 373 of Copper-transporting ATPase 2

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-transporting ATPase 2 between cysteines 1091 and 1104 (60 and 73 respectively in this structure).

Details

Redox score ?
60
PDB code
2koy
Structure name
structure of the e1064a mutant of the n-domain of wilson disease associated protein
Structure deposition date
2009-10-03
Thiol separation (Å)
6
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
10
Peptide accession
P35670
Residue number A
1091
Residue number B
1104
Peptide name
Copper-transporting ATPase 2

Ligandability

Cysteine 1091 of Copper-transporting ATPase 2

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 1104 of Copper-transporting ATPase 2

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-transporting ATPase 2 between cysteines 268 and 271 (31 and 34 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
2rop
Structure name
solution structure of domains 3 and 4 of human atp7b
Structure deposition date
2008-04-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
34
Minimum pKa ?
9
% buried
6
Peptide accession
P35670
Residue number A
268
Residue number B
271
Peptide name
Copper-transporting ATPase 2

Ligandability

Cysteine 268 of Copper-transporting ATPase 2

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 271 of Copper-transporting ATPase 2

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-transporting ATPase 2 between cysteines 499 and 502 (15 and 18 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
2ew9
Structure name
solution structure of apowln5-6
Structure deposition date
2005-11-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
38
Minimum pKa ?
9
% buried
0
Peptide accession
P35670
Residue number A
499
Residue number B
502
Peptide name
Copper-transporting ATPase 2

Ligandability

Cysteine 499 of Copper-transporting ATPase 2

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 502 of Copper-transporting ATPase 2

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-transporting ATPase 2 between cysteines 108 and 113 (57 and 62 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
2n7y
Structure name
nmr structure of metal-binding domain 1 of atp7b
Structure deposition date
2015-09-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
8
% buried
8
Peptide accession
P35670
Residue number A
108
Residue number B
113
Peptide name
Copper-transporting ATPase 2

Ligandability

Cysteine 108 of Copper-transporting ATPase 2

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 113 of Copper-transporting ATPase 2

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-transporting ATPase 2 between cysteines 1104 and 1189. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
2arf
Structure name
solution structure of the wilson atpase n-domain in the presence of atp
Structure deposition date
2005-08-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
54
Peptide accession
P35670
Residue number A
1104
Residue number B
1189
Peptide name
Copper-transporting ATPase 2

Ligandability

Cysteine 1104 of Copper-transporting ATPase 2

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 1189 of Copper-transporting ATPase 2

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.

If this tool was useful for finding a disulphide, please cite: