Superoxide dismutase 1 copper chaperone

Intermolecular

Cysteine 147 of Superoxide dismutase [Cu-Zn] and cysteine 231 L

Cysteine 58 of Superoxide dismutase [Cu-Zn] and cysteine 231

A redox-regulated disulphide may form between cysteine 147 of Superoxide dismutase [Cu-Zn] and cysteine 231 of Superoxide dismutase 1 copper chaperone (146 and 231 respectively in this structure).

Details

Redox score ?

PDB code

5u9m

Structure name

copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper-ion entry site

Structure deposition date

2016-12-16

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Superoxide dismutase [Cu-Zn]

Peptide B name

Superoxide dismutase 1 copper chaperone

Peptide A accession

P00441

Peptide B accession

P40202

Peptide A residue number

147

Peptide B residue number

231

Ligandability

Cysteine 147 of Superoxide dismutase [Cu-Zn]

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.

Ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 231 of Superoxide dismutase 1 copper chaperone

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 between cysteine 58 of Superoxide dismutase [Cu-Zn] and cysteine 231 of Superoxide dismutase 1 copper chaperone (57 and 231 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?