ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Hemojuvelin

Intramolecular
Cysteine 80 and cysteine 119
Cysteine 37 and cysteine 97
Cysteine 42 and cysteine 89
Cysteine 42 and cysteine 97
Cysteine 37 and cysteine 42
Cysteine 89 and cysteine 97
Cysteine 37 and cysteine 89
A redox-regulated disulphide may form within Hemojuvelin between cysteines 80 and 119.

Details

Redox score ?
87
PDB code
4ui1
Structure name
crystal structure of the human rgmc-bmp2 complex
Structure deposition date
2015-03-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6ZVN8
Residue number A
80
Residue number B
119
Peptide name
Hemojuvelin

Ligandability

Cysteine 80 of Hemojuvelin

Cysteine 119 of Hemojuvelin

A redox-regulated disulphide may form within Hemojuvelin between cysteines 37 and 97.

Details

Redox score ?
86
PDB code
4ui1
Structure name
crystal structure of the human rgmc-bmp2 complex
Structure deposition date
2015-03-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6ZVN8
Residue number A
37
Residue number B
97
Peptide name
Hemojuvelin

Ligandability

Cysteine 37 of Hemojuvelin

Cysteine 97 of Hemojuvelin

A redox-regulated disulphide may form within Hemojuvelin between cysteines 42 and 89.

Details

Redox score ?
82
PDB code
4ui1
Structure name
crystal structure of the human rgmc-bmp2 complex
Structure deposition date
2015-03-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6ZVN8
Residue number A
42
Residue number B
89
Peptide name
Hemojuvelin

Ligandability

Cysteine 42 of Hemojuvelin

Cysteine 89 of Hemojuvelin

A redox-regulated disulphide may form within Hemojuvelin between cysteines 42 and 97. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
4ui1
Structure name
crystal structure of the human rgmc-bmp2 complex
Structure deposition date
2015-03-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6ZVN8
Residue number A
42
Residue number B
97
Peptide name
Hemojuvelin

Ligandability

Cysteine 42 of Hemojuvelin

Cysteine 97 of Hemojuvelin

A redox-regulated disulphide may form within Hemojuvelin between cysteines 37 and 42. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
4ui1
Structure name
crystal structure of the human rgmc-bmp2 complex
Structure deposition date
2015-03-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6ZVN8
Residue number A
37
Residue number B
42
Peptide name
Hemojuvelin

Ligandability

Cysteine 37 of Hemojuvelin

Cysteine 42 of Hemojuvelin

A redox-regulated disulphide may form within Hemojuvelin between cysteines 89 and 97. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4ui1
Structure name
crystal structure of the human rgmc-bmp2 complex
Structure deposition date
2015-03-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6ZVN8
Residue number A
89
Residue number B
97
Peptide name
Hemojuvelin

Ligandability

Cysteine 89 of Hemojuvelin

Cysteine 97 of Hemojuvelin

A redox-regulated disulphide may form within Hemojuvelin between cysteines 37 and 89. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4ui1
Structure name
crystal structure of the human rgmc-bmp2 complex
Structure deposition date
2015-03-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6ZVN8
Residue number A
37
Residue number B
89
Peptide name
Hemojuvelin

Ligandability

Cysteine 37 of Hemojuvelin

Cysteine 89 of Hemojuvelin

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