ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Kelch repeat and BTB domain-containing protein 12

Intramolecular
Cysteine 557 and cysteine 599
Cysteine 279 and cysteine 599
Cysteine 279 and cysteine 557
Cysteine 300 and cysteine 599
Cysteine 279 and cysteine 300
Cysteine 300 and cysteine 557
A redox-regulated disulphide may form within Kelch repeat and BTB domain-containing protein 12 between cysteines 557 and 599.

Details

Redox score ?
72
PDB code
7qzq
Structure name
crystal structure of the kelch domain of human kbtbd12
Structure deposition date
2022-01-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
99
Minimum pKa ?
5
% buried
100
Peptide accession
Q3ZCT8
Residue number A
557
Residue number B
599
Peptide name
Kelch repeat and BTB domain-containing protein 12

Ligandability

Cysteine 557 of Kelch repeat and BTB domain-containing protein 12

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 599 of Kelch repeat and BTB domain-containing protein 12

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 Kelch repeat and BTB domain-containing protein 12 between cysteines 279 and 599.

Details

Redox score ?
70
PDB code
7qzq
Structure name
crystal structure of the kelch domain of human kbtbd12
Structure deposition date
2022-01-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
99
Minimum pKa ?
5
% buried
100
Peptide accession
Q3ZCT8
Residue number A
279
Residue number B
599
Peptide name
Kelch repeat and BTB domain-containing protein 12

Ligandability

Cysteine 279 of Kelch repeat and BTB domain-containing protein 12

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 599 of Kelch repeat and BTB domain-containing protein 12

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 Kelch repeat and BTB domain-containing protein 12 between cysteines 279 and 557. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
7qzq
Structure name
crystal structure of the kelch domain of human kbtbd12
Structure deposition date
2022-01-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
105
Minimum pKa ?
14
% buried
100
Peptide accession
Q3ZCT8
Residue number A
279
Residue number B
557
Peptide name
Kelch repeat and BTB domain-containing protein 12

Ligandability

Cysteine 279 of Kelch repeat and BTB domain-containing protein 12

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 557 of Kelch repeat and BTB domain-containing protein 12

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 Kelch repeat and BTB domain-containing protein 12 between cysteines 300 and 599. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
7qzq
Structure name
crystal structure of the kelch domain of human kbtbd12
Structure deposition date
2022-01-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
5
% buried
100
Peptide accession
Q3ZCT8
Residue number A
300
Residue number B
599
Peptide name
Kelch repeat and BTB domain-containing protein 12

Ligandability

Cysteine 300 of Kelch repeat and BTB domain-containing protein 12

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 599 of Kelch repeat and BTB domain-containing protein 12

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 Kelch repeat and BTB domain-containing protein 12 between cysteines 279 and 300. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7qzq
Structure name
crystal structure of the kelch domain of human kbtbd12
Structure deposition date
2022-01-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
95
Minimum pKa ?
13
% buried
100
Peptide accession
Q3ZCT8
Residue number A
279
Residue number B
300
Peptide name
Kelch repeat and BTB domain-containing protein 12

Ligandability

Cysteine 279 of Kelch repeat and BTB domain-containing protein 12

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 300 of Kelch repeat and BTB domain-containing protein 12

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 Kelch repeat and BTB domain-containing protein 12 between cysteines 300 and 557. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
7qzq
Structure name
crystal structure of the kelch domain of human kbtbd12
Structure deposition date
2022-01-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
96
Minimum pKa ?
13
% buried
100
Peptide accession
Q3ZCT8
Residue number A
300
Residue number B
557
Peptide name
Kelch repeat and BTB domain-containing protein 12

Ligandability

Cysteine 300 of Kelch repeat and BTB domain-containing protein 12

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 557 of Kelch repeat and BTB domain-containing protein 12

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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