Alpha-globin

Intramolecular

A redox-regulated disulphide may form within Alpha-globin between cysteines 35 and 105 (34 and 104 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

5ker

Structure name

deer mouse recombinant hemoglobin from high altitude species

Structure deposition date

2016-06-10

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

A4ZQ87

Residue number A

Residue number B

105

Peptide name

Alpha-globin

Ligandability

Cysteine 35 of Alpha-globin

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.