Hemoglobin subunit beta

Intermolecular

Cysteine 104 of Hemoglobin subunit alpha and cysteine 112

Cysteine 105 of Hemoglobin subunit zeta and cysteine 113

A redox-regulated disulphide may form between two units of Hemoglobin subunit beta at cysteines 113 and 113 (112 and 112 respectively in this structure).

Details

Redox score ?

PDB code

1cbl

Structure name

the 1

Structure deposition date

1993-02-18

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide A name

Hemoglobin subunit beta

Peptide B name

Hemoglobin subunit beta

Peptide A accession

P68871

Peptide B accession

P68871

Peptide A residue number

113

Peptide B residue number

113

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 between cysteine 104 of Hemoglobin subunit alpha and cysteine 112 of Hemoglobin subunit beta. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2b7h

Structure name

hemoglobin from cerdocyon thous, a canidae from brazil, at 2

Structure deposition date

2005-10-04

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide A name

Hemoglobin subunit alpha

Peptide B name

Hemoglobin subunit beta

Peptide A accession

P60523

Peptide B accession

P60526

Peptide A residue number

104

Peptide B residue number

112

Ligandability

Cysteine 104 of Hemoglobin subunit alpha

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 112 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.

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. ?