ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Hemoglobin subunit alpha

Intermolecular
Cysteine 104 and cysteine 112 of Hemoglobin subunit beta
Cysteine 105 and cysteine 113 of Hemoglobin subunit delta
Cysteine 105 and cysteine 113 of Hemoglobin subunit beta
Intramolecular
Cysteine 104 and cysteine 111
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 ?
30
PDB code
2b7h
Structure name
hemoglobin from cerdocyon thous, a canidae from brazil, at 2
Structure deposition date
2005-10-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
12
% 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 alpha and cysteine 113 of Hemoglobin subunit delta (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 ?
28
PDB code
1si4
Structure name
crystal structure of human hemoglobin a2 (in r2 state) at 2
Structure deposition date
2004-02-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
100
Peptide A name
Hemoglobin subunit alpha
Peptide B name
Hemoglobin subunit delta
Peptide A accession
P69905
Peptide B accession
P02042
Peptide A residue number
105
Peptide B residue number
113

Ligandability

Cysteine 105 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 113 of Hemoglobin subunit delta

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 alpha 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 ?
27
PDB code
7k4m
Structure name
crystal structure of metap2 modified hemoglobin s
Structure deposition date
2020-09-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
100
Peptide A name
Hemoglobin subunit alpha
Peptide B name
Hemoglobin subunit beta
Peptide A accession
P69905
Peptide B accession
A0A481SHK9
Peptide A residue number
105
Peptide B residue number
113

Ligandability

Cysteine 105 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 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.

A redox-regulated disulphide may form within Hemoglobin subunit alpha between cysteines 104 and 111. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
2b7h
Structure name
hemoglobin from cerdocyon thous, a canidae from brazil, at 2
Structure deposition date
2005-10-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
96
Peptide accession
P60523
Residue number A
104
Residue number B
111
Peptide name
Hemoglobin subunit alpha

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 111 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.

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