a tool for identifying drug-targetable redox-active disulphides

Hemoglobin subunit zeta

Intermolecular

Cysteine 105 and cysteine 113 of Hemoglobin subunit beta

A redox-regulated disulphide may form between cysteine 105 of Hemoglobin subunit zeta and cysteine 113 of Hemoglobin subunit beta (104 and 112 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

29

PDB code

Structure name

human zeta-2 beta-2-s hemoglobin

Structure deposition date

2013-01-16

Thiol separation (Å)

9

Half-sphere exposure sum ?

86

Minimum pK_a ?

12

% buried

100

Peptide A name

Hemoglobin subunit zeta

Peptide B name

Hemoglobin subunit beta

Peptide A accession

Peptide B accession

Peptide A residue number

105

Peptide B residue number

113

Ligandability

Cysteine 105 of Hemoglobin subunit zeta

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.

Cysteine 113 of Hemoglobin subunit beta

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.

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