Actin, alpha skeletal muscle

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Actin, alpha skeletal muscle at cysteines 376 and 376 (374 and 374 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

1rfq

Structure name

actin crystal dynamics: structural implications for f-actin nucleation, polymerization and branching mediated by the anti-parallel dimer

Structure deposition date

2003-11-10

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Actin, alpha skeletal muscle

Peptide B name

Actin, alpha skeletal muscle

Peptide A accession

P68135

Peptide B accession

P68135

Peptide A residue number

376

Peptide B residue number

376

Ligandability

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 Actin, alpha skeletal muscle between cysteines 219 and 259 (217 and 257 respectively in this structure).

Details

Redox score ?

PDB code

3u9d

Structure name

crystal structure of a chimera containing the n-terminal domain (residues 8-24) of drosophila ciboulot and the c-terminal domain (residues 13-44) of bovine thymosin-beta4, bound to g-actin-atp

Structure deposition date

2011-10-18

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide accession

P68136

Residue number A

219

Residue number B