ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Alpha-actinin-2

Intermolecular
Cysteine 270 and cysteine 862
Intramolecular
Cysteine 483 and cysteine 487
A redox-regulated disulphide may form between two units of Alpha-actinin-2 at cysteines 270 and 862. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7ank
Structure name
crystal structure of sarcomeric protein fatz-1 (d91-fatz-1 construct) in complex with half dimer of alpha-actinin-2
Structure deposition date
2020-10-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
44
Peptide A name
Alpha-actinin-2
Peptide B name
Alpha-actinin-2
Peptide A accession
P35609
Peptide B accession
P35609
Peptide A residue number
270
Peptide B residue number
862

Ligandability

Cysteine 270 of Alpha-actinin-2

Cysteine 862 of Alpha-actinin-2

A redox-regulated disulphide may form within Alpha-actinin-2 between cysteines 483 and 487 (96 and 100 respectively in this structure).

Details

Redox score ?
72
PDB code
1quu
Structure name
crystal structure of two central spectrin-like repeats from alpha- actinin
Structure deposition date
1999-07-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
39
Peptide accession
P35609
Residue number A
483
Residue number B
487
Peptide name
Alpha-actinin-2

Ligandability

Cysteine 483 of Alpha-actinin-2

Cysteine 487 of Alpha-actinin-2

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