ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Leptin receptor

Intramolecular
Cysteine 604 and cysteine 1001
Cysteine 604 and cysteine 701
Cysteine 488 and cysteine 498
Cysteine 436 and cysteine 447
Cysteine 473 and cysteine 528
Cysteine 447 and cysteine 498
Cysteine 447 and cysteine 488
Cysteine 436 and cysteine 498
Cysteine 436 and cysteine 488
A redox-regulated disulphide may form within Leptin receptor between cysteines 604 and 1001.

Details

Redox score ?
88
PDB code
3v6o
Structure name
leptin receptor-antibody complex
Structure deposition date
2011-12-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P48357
Residue number A
604
Residue number B
1001
Peptide name
Leptin receptor

Ligandability

Cysteine 604 of Leptin 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 1001 of Leptin 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 1001 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Leptin receptor between cysteines 604 and 701.

Details

Redox score ?
88
PDB code
3v6o
Structure name
leptin receptor-antibody complex
Structure deposition date
2011-12-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P48357
Residue number A
604
Residue number B
701
Peptide name
Leptin receptor

Ligandability

Cysteine 604 of Leptin 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 701 of Leptin 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 701 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Leptin receptor between cysteines 488 and 498.

Details

Redox score ?
87
PDB code
3v6o
Structure name
leptin receptor-antibody complex
Structure deposition date
2011-12-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P48357
Residue number A
488
Residue number B
498
Peptide name
Leptin receptor

Ligandability

Cysteine 488 of Leptin 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 498 of Leptin 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 Leptin receptor between cysteines 436 and 447.

Details

Redox score ?
84
PDB code
3v6o
Structure name
leptin receptor-antibody complex
Structure deposition date
2011-12-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P48357
Residue number A
436
Residue number B
447
Peptide name
Leptin receptor

Ligandability

Cysteine 436 of Leptin 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 447 of Leptin 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 Leptin receptor between cysteines 473 and 528.

Details

Redox score ?
83
PDB code
3v6o
Structure name
leptin receptor-antibody complex
Structure deposition date
2011-12-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P48357
Residue number A
473
Residue number B
528
Peptide name
Leptin receptor

Ligandability

Cysteine 473 of Leptin 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 528 of Leptin 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 Leptin receptor between cysteines 447 and 498. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
3v6o
Structure name
leptin receptor-antibody complex
Structure deposition date
2011-12-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P48357
Residue number A
447
Residue number B
498
Peptide name
Leptin receptor

Ligandability

Cysteine 447 of Leptin 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 498 of Leptin 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 Leptin receptor between cysteines 447 and 488. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
3v6o
Structure name
leptin receptor-antibody complex
Structure deposition date
2011-12-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P48357
Residue number A
447
Residue number B
488
Peptide name
Leptin receptor

Ligandability

Cysteine 447 of Leptin 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 488 of Leptin 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 Leptin receptor between cysteines 436 and 498. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
3v6o
Structure name
leptin receptor-antibody complex
Structure deposition date
2011-12-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P48357
Residue number A
436
Residue number B
498
Peptide name
Leptin receptor

Ligandability

Cysteine 436 of Leptin 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 498 of Leptin 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 Leptin receptor between cysteines 436 and 488. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
3v6o
Structure name
leptin receptor-antibody complex
Structure deposition date
2011-12-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P48357
Residue number A
436
Residue number B
488
Peptide name
Leptin receptor

Ligandability

Cysteine 436 of Leptin 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 488 of Leptin 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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