Relaxin-3
Intermolecular
Cysteine 47 and cysteine 135 of Insulin-like peptide INSL5
Cysteine 47 and cysteine 142
Cysteine 35 and cysteine 122 of Insulin-like peptide INSL5
Cysteine 35 and cysteine 129
Cysteine 35 and cysteine 121 of Insulin-like peptide INSL5
Cysteine 35 and cysteine 126 of Insulin-like peptide INSL5
Cysteine 35 and cysteine 128
Cysteine 35 and cysteine 133
Intramolecular
Cysteine 128 and cysteine 133
Cysteine 128 and cysteine 129
Cysteine 129 and cysteine 133
2k1v B 22 A 24
A redox-regulated disulphide may form between cysteine 47 of Relaxin-3 and cysteine 135 of Insulin-like peptide INSL5 (22 and 24 respectively in this structure).
Details
Redox score ?
91
PDB code
2k1v
Structure name
r3/i5 relaxin chimera
Structure deposition date
2008-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
Relaxin-3
Peptide B name
Insulin-like peptide INSL5
Peptide A accession
Q8WXF3
Peptide B accession
Q9Y5Q6
Peptide A residue number
47
Peptide B residue number
135
Ligandability
Cysteine 47 of Relaxin-3
Cysteine 135 of Insulin-like peptide INSL5
2fhw B 22 A 24
A redox-regulated disulphide may form between two units of Relaxin-3 at cysteines 47 and 142 (22 and 24 respectively in this structure).
Details
Redox score ?
88
PDB code
2fhw
Structure name
solution structure of human relaxin-3
Structure deposition date
2005-12-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
Relaxin-3
Peptide B name
Relaxin-3
Peptide A accession
Q8WXF3
Peptide B accession
Q8WXF3
Peptide A residue number
47
Peptide B residue number
142
Ligandability
Cysteine 47 of Relaxin-3
Cysteine 142 of Relaxin-3
2k1v B 10 A 11
A redox-regulated disulphide may form between cysteine 35 of Relaxin-3 and cysteine 122 of Insulin-like peptide INSL5 (10 and 11 respectively in this structure).
Details
Redox score ?
85
PDB code
2k1v
Structure name
r3/i5 relaxin chimera
Structure deposition date
2008-03-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide A name
Relaxin-3
Peptide B name
Insulin-like peptide INSL5
Peptide A accession
Q8WXF3
Peptide B accession
Q9Y5Q6
Peptide A residue number
35
Peptide B residue number
122
Ligandability
Cysteine 35 of Relaxin-3
Cysteine 122 of Insulin-like peptide INSL5
2fhw B 10 A 11
A redox-regulated disulphide may form between two units of Relaxin-3 at cysteines 35 and 129 (10 and 11 respectively in this structure).
Details
Redox score ?
82
PDB code
2fhw
Structure name
solution structure of human relaxin-3
Structure deposition date
2005-12-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide A name
Relaxin-3
Peptide B name
Relaxin-3
Peptide A accession
Q8WXF3
Peptide B accession
Q8WXF3
Peptide A residue number
35
Peptide B residue number
129
Ligandability
Cysteine 35 of Relaxin-3
Cysteine 129 of Relaxin-3
2k1v B 10 A 10
A redox-regulated disulphide may form between cysteine 35 of Relaxin-3 and cysteine 121 of Insulin-like peptide INSL5 (10 and 10 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
2k1v
Structure name
r3/i5 relaxin chimera
Structure deposition date
2008-03-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide A name
Relaxin-3
Peptide B name
Insulin-like peptide INSL5
Peptide A accession
Q8WXF3
Peptide B accession
Q9Y5Q6
Peptide A residue number
35
Peptide B residue number
121
Ligandability
Cysteine 35 of Relaxin-3
Cysteine 121 of Insulin-like peptide INSL5
2k1v B 10 A 15
A redox-regulated disulphide may form between cysteine 35 of Relaxin-3 and cysteine 126 of Insulin-like peptide INSL5 (10 and 15 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
2k1v
Structure name
r3/i5 relaxin chimera
Structure deposition date
2008-03-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide A name
Relaxin-3
Peptide B name
Insulin-like peptide INSL5
Peptide A accession
Q8WXF3
Peptide B accession
Q9Y5Q6
Peptide A residue number
35
Peptide B residue number
126
Ligandability
Cysteine 35 of Relaxin-3
Cysteine 126 of Insulin-like peptide INSL5
2fhw B 10 A 10
A redox-regulated disulphide may form between two units of Relaxin-3 at cysteines 35 and 128 (10 and 10 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
2fhw
Structure name
solution structure of human relaxin-3
Structure deposition date
2005-12-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide A name
Relaxin-3
Peptide B name
Relaxin-3
Peptide A accession
Q8WXF3
Peptide B accession
Q8WXF3
Peptide A residue number
35
Peptide B residue number
128
Ligandability
Cysteine 35 of Relaxin-3
Cysteine 128 of Relaxin-3
2fhw B 10 A 15
A redox-regulated disulphide may form between two units of Relaxin-3 at cysteines 35 and 133 (10 and 15 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
2fhw
Structure name
solution structure of human relaxin-3
Structure deposition date
2005-12-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide A name
Relaxin-3
Peptide B name
Relaxin-3
Peptide A accession
Q8WXF3
Peptide B accession
Q8WXF3
Peptide A residue number
35
Peptide B residue number
133
Ligandability
Cysteine 35 of Relaxin-3
Cysteine 133 of Relaxin-3
2fhw A 10 A 15
A redox-regulated disulphide may form within Relaxin-3 between cysteines 128 and 133 (10 and 15 respectively in this structure).
Details
Redox score ?
87
PDB code
2fhw
Structure name
solution structure of human relaxin-3
Structure deposition date
2005-12-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8WXF3
Residue number A
128
Residue number B
133
Peptide name
Relaxin-3
Ligandability
Cysteine 128 of Relaxin-3
Cysteine 133 of Relaxin-3
2fhw A 10 A 11
A redox-regulated disulphide may form within Relaxin-3 between cysteines 128 and 129 (10 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 ?
46
PDB code
2fhw
Structure name
solution structure of human relaxin-3
Structure deposition date
2005-12-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8WXF3
Residue number A
128
Residue number B
129
Peptide name
Relaxin-3
Ligandability
Cysteine 128 of Relaxin-3
Cysteine 129 of Relaxin-3
2fhw A 11 A 15
A redox-regulated disulphide may form within Relaxin-3 between cysteines 129 and 133 (11 and 15 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
2fhw
Structure name
solution structure of human relaxin-3
Structure deposition date
2005-12-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8WXF3
Residue number A
129
Residue number B
133
Peptide name
Relaxin-3
Ligandability
Cysteine 129 of Relaxin-3
Cysteine 133 of Relaxin-3
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