Prorelaxin H2
Intermolecular
Cysteine 185 and cysteine 47
Cysteine 172 and cysteine 35
Cysteine 171 and cysteine 35
Cysteine 176 and cysteine 35
Intramolecular
Cysteine 171 and cysteine 176
Cysteine 171 and cysteine 172
Cysteine 176 and cysteine 185
Cysteine 172 and cysteine 176
6rlx C 20 D 19
A redox-regulated disulphide may form between two units of Prorelaxin H2 at cysteines 185 and 47 (20 and 19 respectively in this structure).
Details
Redox score ?
90
PDB code
6rlx
Structure name
x-ray structure of human relaxin at 1
Structure deposition date
1991-06-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
Prorelaxin H2
Peptide B name
Prorelaxin H2
Peptide A accession
P04090
Peptide B accession
P04090
Peptide A residue number
185
Peptide B residue number
47
Ligandability
Cysteine 185 of Prorelaxin H2
Cysteine 47 of Prorelaxin H2
6rlx C 7 D 7
A redox-regulated disulphide may form between two units of Prorelaxin H2 at cysteines 172 and 35 (7 and 7 respectively in this structure).
Details
Redox score ?
84
PDB code
6rlx
Structure name
x-ray structure of human relaxin at 1
Structure deposition date
1991-06-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide A name
Prorelaxin H2
Peptide B name
Prorelaxin H2
Peptide A accession
P04090
Peptide B accession
P04090
Peptide A residue number
172
Peptide B residue number
35
Ligandability
Cysteine 172 of Prorelaxin H2
Cysteine 35 of Prorelaxin H2
6rlx C 6 D 7
A redox-regulated disulphide may form between two units of Prorelaxin H2 at cysteines 171 and 35 (6 and 7 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
6rlx
Structure name
x-ray structure of human relaxin at 1
Structure deposition date
1991-06-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide A name
Prorelaxin H2
Peptide B name
Prorelaxin H2
Peptide A accession
P04090
Peptide B accession
P04090
Peptide A residue number
171
Peptide B residue number
35
Ligandability
Cysteine 171 of Prorelaxin H2
Cysteine 35 of Prorelaxin H2
6rlx C 11 D 7
A redox-regulated disulphide may form between two units of Prorelaxin H2 at cysteines 176 and 35 (11 and 7 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
6rlx
Structure name
x-ray structure of human relaxin at 1
Structure deposition date
1991-06-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide A name
Prorelaxin H2
Peptide B name
Prorelaxin H2
Peptide A accession
P04090
Peptide B accession
P04090
Peptide A residue number
176
Peptide B residue number
35
Ligandability
Cysteine 176 of Prorelaxin H2
Cysteine 35 of Prorelaxin H2
6rlx C 6 C 11
A redox-regulated disulphide may form within Prorelaxin H2 between cysteines 171 and 176 (6 and 11 respectively in this structure).
Details
Redox score ?
85
PDB code
6rlx
Structure name
x-ray structure of human relaxin at 1
Structure deposition date
1991-06-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04090
Residue number A
171
Residue number B
176
Peptide name
Prorelaxin H2
Ligandability
Cysteine 171 of Prorelaxin H2
Cysteine 176 of Prorelaxin H2
6rlx C 6 C 7
A redox-regulated disulphide may form within Prorelaxin H2 between cysteines 171 and 172 (6 and 7 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
6rlx
Structure name
x-ray structure of human relaxin at 1
Structure deposition date
1991-06-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04090
Residue number A
171
Residue number B
172
Peptide name
Prorelaxin H2
Ligandability
Cysteine 171 of Prorelaxin H2
Cysteine 172 of Prorelaxin H2
2mv1 A 15 A 24
A redox-regulated disulphide may form within Prorelaxin H2 between cysteines 176 and 185 (15 and 24 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
2mv1
Structure name
solution nmr structure of human relaxin-2
Structure deposition date
2014-09-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04090
Residue number A
176
Residue number B
185
Peptide name
Prorelaxin H2
Ligandability
Cysteine 176 of Prorelaxin H2
Cysteine 185 of Prorelaxin H2
6rlx A 7 A 11
A redox-regulated disulphide may form within Prorelaxin H2 between cysteines 172 and 176 (7 and 11 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
6rlx
Structure name
x-ray structure of human relaxin at 1
Structure deposition date
1991-06-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04090
Residue number A
172
Residue number B
176
Peptide name
Prorelaxin H2
Ligandability
Cysteine 172 of Prorelaxin H2
Cysteine 176 of Prorelaxin H2
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