ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

F-actin-capping protein subunit alpha-1

Intramolecular
Cysteine 141 and cysteine 157
Cysteine 124 and cysteine 141 L
A redox-regulated disulphide may form within F-actin-capping protein subunit alpha-1 between cysteines 141 and 157. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
5afu
Structure name
cryo-em structure of dynein tail-dynactin-bicd2n complex
Structure deposition date
2015-01-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
100
Peptide accession
A0PFK5
Residue number A
141
Residue number B
157
Peptide name
F-actin-capping protein subunit alpha-1

Ligandability

Cysteine 141 of F-actin-capping protein subunit alpha-1

Cysteine 157 of F-actin-capping protein subunit alpha-1

A redox-regulated disulphide may form within F-actin-capping protein subunit alpha-1 between cysteines 124 and 141. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
6f1t
Structure name
cryo-em structure of two dynein tail domains bound to dynactin and bicdr1
Structure deposition date
2017-11-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
13
% buried
93
Peptide accession
A0PFK5
Residue number A
124
Residue number B
141
Peptide name
F-actin-capping protein subunit alpha-1

Ligandability

Cysteine 124 of F-actin-capping protein subunit alpha-1

Cysteine 141 of F-actin-capping protein subunit alpha-1

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