ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase RNF123

Intramolecular
Cysteine 1288 and cysteine 1291
Cysteine 1269 and cysteine 1291
Cysteine 1254 and cysteine 1257
Cysteine 1254 and cysteine 1277
Cysteine 1254 and cysteine 1274
Cysteine 1269 and cysteine 1288
Cysteine 1257 and cysteine 1274
Cysteine 1274 and cysteine 1277
Cysteine 1257 and cysteine 1277
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF123 between cysteines 1288 and 1291 (45 and 48 respectively in this structure).

Details

Redox score ?
87
PDB code
2ma6
Structure name
solution nmr structure of the ring finger domain from the kip1 ubiquitination-promoting e3 complex protein 1 (kpc1/rnf123) from homo sapiens, northeast structural genomics consortium (nesg) target hr8700a
Structure deposition date
2013-06-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
5
% buried
5
Peptide accession
Q5XPI4
Residue number A
1288
Residue number B
1291
Peptide name
E3 ubiquitin-protein ligase RNF123

Ligandability

Cysteine 1288 of E3 ubiquitin-protein ligase RNF123

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 1291 of E3 ubiquitin-protein ligase RNF123

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 E3 ubiquitin-protein ligase RNF123 between cysteines 1269 and 1291 (26 and 48 respectively in this structure).

Details

Redox score ?
87
PDB code
2ma6
Structure name
solution nmr structure of the ring finger domain from the kip1 ubiquitination-promoting e3 complex protein 1 (kpc1/rnf123) from homo sapiens, northeast structural genomics consortium (nesg) target hr8700a
Structure deposition date
2013-06-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
34
Minimum pKa ?
5
% buried
0
Peptide accession
Q5XPI4
Residue number A
1269
Residue number B
1291
Peptide name
E3 ubiquitin-protein ligase RNF123

Ligandability

Cysteine 1269 of E3 ubiquitin-protein ligase RNF123

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 1291 of E3 ubiquitin-protein ligase RNF123

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 E3 ubiquitin-protein ligase RNF123 between cysteines 1254 and 1257 (11 and 14 respectively in this structure).

Details

Redox score ?
85
PDB code
2ma6
Structure name
solution nmr structure of the ring finger domain from the kip1 ubiquitination-promoting e3 complex protein 1 (kpc1/rnf123) from homo sapiens, northeast structural genomics consortium (nesg) target hr8700a
Structure deposition date
2013-06-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
8
Peptide accession
Q5XPI4
Residue number A
1254
Residue number B
1257
Peptide name
E3 ubiquitin-protein ligase RNF123

Ligandability

Cysteine 1254 of E3 ubiquitin-protein ligase RNF123

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 1257 of E3 ubiquitin-protein ligase RNF123

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 E3 ubiquitin-protein ligase RNF123 between cysteines 1254 and 1277 (11 and 34 respectively in this structure).

Details

Redox score ?
84
PDB code
2ma6
Structure name
solution nmr structure of the ring finger domain from the kip1 ubiquitination-promoting e3 complex protein 1 (kpc1/rnf123) from homo sapiens, northeast structural genomics consortium (nesg) target hr8700a
Structure deposition date
2013-06-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
6
% buried
16
Peptide accession
Q5XPI4
Residue number A
1254
Residue number B
1277
Peptide name
E3 ubiquitin-protein ligase RNF123

Ligandability

Cysteine 1254 of E3 ubiquitin-protein ligase RNF123

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 1277 of E3 ubiquitin-protein ligase RNF123

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 E3 ubiquitin-protein ligase RNF123 between cysteines 1254 and 1274 (11 and 31 respectively in this structure).

Details

Redox score ?
83
PDB code
2ma6
Structure name
solution nmr structure of the ring finger domain from the kip1 ubiquitination-promoting e3 complex protein 1 (kpc1/rnf123) from homo sapiens, northeast structural genomics consortium (nesg) target hr8700a
Structure deposition date
2013-06-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
6
% buried
14
Peptide accession
Q5XPI4
Residue number A
1254
Residue number B
1274
Peptide name
E3 ubiquitin-protein ligase RNF123

Ligandability

Cysteine 1254 of E3 ubiquitin-protein ligase RNF123

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 1274 of E3 ubiquitin-protein ligase RNF123

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 E3 ubiquitin-protein ligase RNF123 between cysteines 1269 and 1288 (26 and 45 respectively in this structure).

Details

Redox score ?
81
PDB code
2ma6
Structure name
solution nmr structure of the ring finger domain from the kip1 ubiquitination-promoting e3 complex protein 1 (kpc1/rnf123) from homo sapiens, northeast structural genomics consortium (nesg) target hr8700a
Structure deposition date
2013-06-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
5
Peptide accession
Q5XPI4
Residue number A
1269
Residue number B
1288
Peptide name
E3 ubiquitin-protein ligase RNF123

Ligandability

Cysteine 1269 of E3 ubiquitin-protein ligase RNF123

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 1288 of E3 ubiquitin-protein ligase RNF123

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 E3 ubiquitin-protein ligase RNF123 between cysteines 1257 and 1274 (14 and 31 respectively in this structure).

Details

Redox score ?
79
PDB code
2ma6
Structure name
solution nmr structure of the ring finger domain from the kip1 ubiquitination-promoting e3 complex protein 1 (kpc1/rnf123) from homo sapiens, northeast structural genomics consortium (nesg) target hr8700a
Structure deposition date
2013-06-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
6
Peptide accession
Q5XPI4
Residue number A
1257
Residue number B
1274
Peptide name
E3 ubiquitin-protein ligase RNF123

Ligandability

Cysteine 1257 of E3 ubiquitin-protein ligase RNF123

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 1274 of E3 ubiquitin-protein ligase RNF123

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 E3 ubiquitin-protein ligase RNF123 between cysteines 1274 and 1277 (31 and 34 respectively in this structure).

Details

Redox score ?
77
PDB code
2ma6
Structure name
solution nmr structure of the ring finger domain from the kip1 ubiquitination-promoting e3 complex protein 1 (kpc1/rnf123) from homo sapiens, northeast structural genomics consortium (nesg) target hr8700a
Structure deposition date
2013-06-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
14
Peptide accession
Q5XPI4
Residue number A
1274
Residue number B
1277
Peptide name
E3 ubiquitin-protein ligase RNF123

Ligandability

Cysteine 1274 of E3 ubiquitin-protein ligase RNF123

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 1277 of E3 ubiquitin-protein ligase RNF123

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 E3 ubiquitin-protein ligase RNF123 between cysteines 1257 and 1277 (14 and 34 respectively in this structure).

Details

Redox score ?
75
PDB code
2ma6
Structure name
solution nmr structure of the ring finger domain from the kip1 ubiquitination-promoting e3 complex protein 1 (kpc1/rnf123) from homo sapiens, northeast structural genomics consortium (nesg) target hr8700a
Structure deposition date
2013-06-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
10
% buried
8
Peptide accession
Q5XPI4
Residue number A
1257
Residue number B
1277
Peptide name
E3 ubiquitin-protein ligase RNF123

Ligandability

Cysteine 1257 of E3 ubiquitin-protein ligase RNF123

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 1277 of E3 ubiquitin-protein ligase RNF123

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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