ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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KN motif and ankyrin repeat domains 1

Intramolecular
Cysteine 1101 and cysteine 1122
Cysteine 1231 and cysteine 1264
Cysteine 1195 and cysteine 1231
A redox-regulated disulphide may form within KN motif and ankyrin repeat domains 1 between cysteines 1101 and 1122. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
7ddx
Structure name
crystal structure of kank1 s1179f mutant in complex wtih eif4a1
Structure deposition date
2020-10-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
45
Peptide accession
E9Q238
Residue number A
1101
Residue number B
1122
Peptide name
KN motif and ankyrin repeat domains 1

Ligandability

Cysteine 1101 of KN motif and ankyrin repeat domains 1

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 1122 of KN motif and ankyrin repeat domains 1

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 KN motif and ankyrin repeat domains 1 between cysteines 1231 and 1264. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7ddx
Structure name
crystal structure of kank1 s1179f mutant in complex wtih eif4a1
Structure deposition date
2020-10-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
28
Peptide accession
E9Q238
Residue number A
1231
Residue number B
1264
Peptide name
KN motif and ankyrin repeat domains 1

Ligandability

Cysteine 1231 of KN motif and ankyrin repeat domains 1

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 1264 of KN motif and ankyrin repeat domains 1

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 KN motif and ankyrin repeat domains 1 between cysteines 1195 and 1231. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
7ddx
Structure name
crystal structure of kank1 s1179f mutant in complex wtih eif4a1
Structure deposition date
2020-10-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
57
Peptide accession
E9Q238
Residue number A
1195
Residue number B
1231
Peptide name
KN motif and ankyrin repeat domains 1

Ligandability

Cysteine 1195 of KN motif and ankyrin repeat domains 1

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 1231 of KN motif and ankyrin repeat domains 1

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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