ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Growth hormone receptor

Intramolecular
Cysteine 101 and cysteine 112
Cysteine 56 and cysteine 66
Cysteine 126 and cysteine 140
Cysteine 66 and cysteine 112
Cysteine 66 and cysteine 101
Cysteine 56 and cysteine 112
A redox-regulated disulphide may form within Growth hormone receptor between cysteines 101 and 112 (83 and 94 respectively in this structure).

Details

Redox score ?
84
PDB code
3hhr
Structure name
human growth hormone and extracellular domain of its receptor: crystal structure of the complex
Structure deposition date
1993-12-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10912
Residue number A
101
Residue number B
112
Peptide name
Growth hormone receptor

Ligandability

Cysteine 101 of Growth hormone receptor

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 Growth hormone receptor

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 Growth hormone receptor between cysteines 56 and 66 (238 and 248 respectively in this structure).

Details

Redox score ?
82
PDB code
1a22
Structure name
human growth hormone bound to single receptor
Structure deposition date
1998-01-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10912
Residue number A
56
Residue number B
66
Peptide name
Growth hormone receptor

Ligandability

Cysteine 56 of Growth hormone receptor

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 66 of Growth hormone receptor

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 Growth hormone receptor between cysteines 126 and 140 (108 and 122 respectively in this structure).

Details

Redox score ?
82
PDB code
3hhr
Structure name
human growth hormone and extracellular domain of its receptor: crystal structure of the complex
Structure deposition date
1993-12-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10912
Residue number A
126
Residue number B
140
Peptide name
Growth hormone receptor

Ligandability

Cysteine 126 of Growth hormone receptor

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 140 of Growth hormone receptor

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 Growth hormone receptor between cysteines 66 and 112 (548 and 594 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
1kf9
Structure name
phage display derived variant of human growth hormone complexed with two copies of the extracellular domain of its receptor
Structure deposition date
2001-11-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10912
Residue number A
66
Residue number B
112
Peptide name
Growth hormone receptor

Ligandability

Cysteine 66 of Growth hormone receptor

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 Growth hormone receptor

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 Growth hormone receptor between cysteines 66 and 101 (48 and 83 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
1hwg
Structure name
1:2 complex of human growth hormone with its soluble binding protein
Structure deposition date
1996-11-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10912
Residue number A
66
Residue number B
101
Peptide name
Growth hormone receptor

Ligandability

Cysteine 66 of Growth hormone receptor

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 101 of Growth hormone receptor

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 Growth hormone receptor between cysteines 56 and 112 (238 and 294 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
1a22
Structure name
human growth hormone bound to single receptor
Structure deposition date
1998-01-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P10912
Residue number A
56
Residue number B
112
Peptide name
Growth hormone receptor

Ligandability

Cysteine 56 of Growth hormone receptor

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 Growth hormone receptor

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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