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a tool for identifying drug-targetable redox-active disulphides

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Low-density lipoprotein receptor-related protein 4

Intramolecular
Cysteine 358 and cysteine 369
Cysteine 399 and cysteine 409
Cysteine 380 and cysteine 393
Cysteine 365 and cysteine 378
Cysteine 709 and cysteine 722
Cysteine 420 and cysteine 433
Cysteine 724 and cysteine 736
Cysteine 405 and cysteine 418
Cysteine 702 and cysteine 713
Cysteine 365 and cysteine 369
More...
Cysteine 405 and cysteine 409
Cysteine 709 and cysteine 713
Cysteine 358 and cysteine 365
Cysteine 369 and cysteine 378
Cysteine 409 and cysteine 418
Cysteine 702 and cysteine 709
Cysteine 358 and cysteine 378
Cysteine 722 and cysteine 736
Cysteine 713 and cysteine 722
Cysteine 709 and cysteine 736
Cysteine 418 and cysteine 433
Cysteine 405 and cysteine 433
Cysteine 399 and cysteine 418
Cysteine 365 and cysteine 380
Cysteine 405 and cysteine 420
Cysteine 378 and cysteine 380
Cysteine 418 and cysteine 420
Cysteine 702 and cysteine 722
Cysteine 399 and cysteine 405
Cysteine 365 and cysteine 393
Cysteine 378 and cysteine 393
Cysteine 709 and cysteine 724
Cysteine 722 and cysteine 724
Cysteine 713 and cysteine 736
A redox-regulated disulphide may form within Low-density lipoprotein receptor-related protein 4 between cysteines 358 and 369.

Details

Redox score ?
91
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
358
Residue number B
369
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 358 of Low-density lipoprotein receptor-related protein 4

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 369 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 399 and 409.

Details

Redox score ?
90
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
399
Residue number B
409
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 399 of Low-density lipoprotein receptor-related protein 4

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 409 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 380 and 393.

Details

Redox score ?
89
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
380
Residue number B
393
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 380 of Low-density lipoprotein receptor-related protein 4

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 393 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 365 and 378.

Details

Redox score ?
88
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
365
Residue number B
378
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 365 of Low-density lipoprotein receptor-related protein 4

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 378 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 709 and 722.

Details

Redox score ?
86
PDB code
3v64
Structure name
crystal structure of agrin and lrp4
Structure deposition date
2011-12-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
709
Residue number B
722
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 709 of Low-density lipoprotein receptor-related protein 4

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 722 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 420 and 433.

Details

Redox score ?
86
PDB code
3v64
Structure name
crystal structure of agrin and lrp4
Structure deposition date
2011-12-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
420
Residue number B
433
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 420 of Low-density lipoprotein receptor-related protein 4

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 433 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 724 and 736.

Details

Redox score ?
86
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
724
Residue number B
736
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 724 of Low-density lipoprotein receptor-related protein 4

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 736 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 405 and 418.

Details

Redox score ?
84
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
405
Residue number B
418
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 405 of Low-density lipoprotein receptor-related protein 4

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 418 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 702 and 713.

Details

Redox score ?
83
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
702
Residue number B
713
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 702 of Low-density lipoprotein receptor-related protein 4

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 713 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 365 and 369.

Details

Redox score ?
81
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
3
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
365
Residue number B
369
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 365 of Low-density lipoprotein receptor-related protein 4

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 369 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 405 and 409.

Details

Redox score ?
78
PDB code
3v64
Structure name
crystal structure of agrin and lrp4
Structure deposition date
2011-12-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9QYP1
Residue number A
405
Residue number B
409
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 405 of Low-density lipoprotein receptor-related protein 4

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 409 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 709 and 713.

Details

Redox score ?
72
PDB code
3v64
Structure name
crystal structure of agrin and lrp4
Structure deposition date
2011-12-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
709
Residue number B
713
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 709 of Low-density lipoprotein receptor-related protein 4

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 713 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 358 and 365.

Details

Redox score ?
72
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
358
Residue number B
365
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 358 of Low-density lipoprotein receptor-related protein 4

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 365 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 369 and 378.

Details

Redox score ?
70
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
5
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
369
Residue number B
378
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 369 of Low-density lipoprotein receptor-related protein 4

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 378 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 409 and 418.

Details

Redox score ?
70
PDB code
3v64
Structure name
crystal structure of agrin and lrp4
Structure deposition date
2011-12-18
Thiol separation (Å)
5
Half-sphere exposure sum ?
39
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9QYP1
Residue number A
409
Residue number B
418
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 409 of Low-density lipoprotein receptor-related protein 4

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 418 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 702 and 709.

Details

Redox score ?
63
PDB code
3v64
Structure name
crystal structure of agrin and lrp4
Structure deposition date
2011-12-18
Thiol separation (Å)
6
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
702
Residue number B
709
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 702 of Low-density lipoprotein receptor-related protein 4

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 709 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 358 and 378.

Details

Redox score ?
62
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
358
Residue number B
378
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 358 of Low-density lipoprotein receptor-related protein 4

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 378 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 722 and 736. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
722
Residue number B
736
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 722 of Low-density lipoprotein receptor-related protein 4

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 736 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 713 and 722. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
6
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
713
Residue number B
722
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 713 of Low-density lipoprotein receptor-related protein 4

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 722 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 709 and 736. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
709
Residue number B
736
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 709 of Low-density lipoprotein receptor-related protein 4

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 736 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 418 and 433. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
418
Residue number B
433
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 418 of Low-density lipoprotein receptor-related protein 4

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 433 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 405 and 433. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
405
Residue number B
433
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 405 of Low-density lipoprotein receptor-related protein 4

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 433 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 399 and 418. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
399
Residue number B
418
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 399 of Low-density lipoprotein receptor-related protein 4

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 418 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 365 and 380. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
365
Residue number B
380
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 365 of Low-density lipoprotein receptor-related protein 4

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 380 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 405 and 420. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
405
Residue number B
420
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 405 of Low-density lipoprotein receptor-related protein 4

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 420 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 378 and 380. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
378
Residue number B
380
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 378 of Low-density lipoprotein receptor-related protein 4

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 380 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 418 and 420. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3v64
Structure name
crystal structure of agrin and lrp4
Structure deposition date
2011-12-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
418
Residue number B
420
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 418 of Low-density lipoprotein receptor-related protein 4

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 420 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 702 and 722. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
702
Residue number B
722
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 702 of Low-density lipoprotein receptor-related protein 4

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 722 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 399 and 405. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
399
Residue number B
405
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 399 of Low-density lipoprotein receptor-related protein 4

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 405 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 365 and 393. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
365
Residue number B
393
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 365 of Low-density lipoprotein receptor-related protein 4

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 393 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 378 and 393. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
378
Residue number B
393
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 378 of Low-density lipoprotein receptor-related protein 4

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 393 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 709 and 724. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
709
Residue number B
724
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 709 of Low-density lipoprotein receptor-related protein 4

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 724 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 722 and 724. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
3v64
Structure name
crystal structure of agrin and lrp4
Structure deposition date
2011-12-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
722
Residue number B
724
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 722 of Low-density lipoprotein receptor-related protein 4

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 724 of Low-density lipoprotein receptor-related protein 4

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 Low-density lipoprotein receptor-related protein 4 between cysteines 713 and 736. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
3v65
Structure name
crystal structure of agrin and lrp4 complex
Structure deposition date
2011-12-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9QYP1
Residue number A
713
Residue number B
736
Peptide name
Low-density lipoprotein receptor-related protein 4

Ligandability

Cysteine 713 of Low-density lipoprotein receptor-related protein 4

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 736 of Low-density lipoprotein receptor-related protein 4

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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