ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Guided entry of tail-anchored proteins factor 1

Intermolecular
Cysteine 157 and cysteine 275 of Guided entry of tail-anchored proteins factor CAMLG
Cysteine 162 and cysteine 275 of Guided entry of tail-anchored proteins factor CAMLG
Intramolecular
Cysteine 157 and cysteine 162
Cysteine 21 and cysteine 162
A redox-regulated disulphide may form between cysteine 157 of Guided entry of tail-anchored proteins factor 1 and cysteine 275 of Guided entry of tail-anchored proteins factor CAMLG. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
6so5
Structure name
homo sapiens wrb/caml heterotetramer in complex with a trc40 dimer
Structure deposition date
2019-08-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
18
Peptide A name
Guided entry of tail-anchored proteins factor 1
Peptide B name
Guided entry of tail-anchored proteins factor CAMLG
Peptide A accession
O00258
Peptide B accession
P49069
Peptide A residue number
157
Peptide B residue number
275

Ligandability

Cysteine 157 of Guided entry of tail-anchored proteins factor 1

Cysteine 275 of Guided entry of tail-anchored proteins factor CAMLG

A redox-regulated disulphide may form between cysteine 162 of Guided entry of tail-anchored proteins factor 1 and cysteine 275 of Guided entry of tail-anchored proteins factor CAMLG. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6so5
Structure name
homo sapiens wrb/caml heterotetramer in complex with a trc40 dimer
Structure deposition date
2019-08-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
52
Peptide A name
Guided entry of tail-anchored proteins factor 1
Peptide B name
Guided entry of tail-anchored proteins factor CAMLG
Peptide A accession
O00258
Peptide B accession
P49069
Peptide A residue number
162
Peptide B residue number
275

Ligandability

Cysteine 162 of Guided entry of tail-anchored proteins factor 1

Cysteine 275 of Guided entry of tail-anchored proteins factor CAMLG

A redox-regulated disulphide may form within Guided entry of tail-anchored proteins factor 1 between cysteines 157 and 162. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
6so5
Structure name
homo sapiens wrb/caml heterotetramer in complex with a trc40 dimer
Structure deposition date
2019-08-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
48
Peptide accession
O00258
Residue number A
157
Residue number B
162
Peptide name
Guided entry of tail-anchored proteins factor 1

Ligandability

Cysteine 157 of Guided entry of tail-anchored proteins factor 1

Cysteine 162 of Guided entry of tail-anchored proteins factor 1

A redox-regulated disulphide may form within Guided entry of tail-anchored proteins factor 1 between cysteines 21 and 162. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
6so5
Structure name
homo sapiens wrb/caml heterotetramer in complex with a trc40 dimer
Structure deposition date
2019-08-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
54
Peptide accession
O00258
Residue number A
21
Residue number B
162
Peptide name
Guided entry of tail-anchored proteins factor 1

Ligandability

Cysteine 21 of Guided entry of tail-anchored proteins factor 1

Cysteine 162 of Guided entry of tail-anchored proteins factor 1

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