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Thrombospondin-2

Intramolecular
Cysteine 577 and cysteine 588
Cysteine 622 and cysteine 646
Cysteine 558 and cysteine 574
Cysteine 553 and cysteine 564
Cysteine 659 and cysteine 678
Cysteine 652 and cysteine 665
Cysteine 594 and cysteine 610
Cysteine 680 and cysteine 691
Cysteine 707 and cysteine 715
Cysteine 601 and cysteine 619
More...
Cysteine 912 and cysteine 932
Cysteine 838 and cysteine 858
Cysteine 876 and cysteine 896
Cysteine 779 and cysteine 799
Cysteine 948 and cysteine 1169
Cysteine 720 and cysteine 740
Cysteine 756 and cysteine 776
Cysteine 815 and cysteine 835
Cysteine 558 and cysteine 564
Cysteine 601 and cysteine 610
Cysteine 659 and cysteine 665
Cysteine 564 and cysteine 574
Cysteine 553 and cysteine 558
Cysteine 610 and cysteine 619
Cysteine 665 and cysteine 678
Cysteine 652 and cysteine 659
Cysteine 594 and cysteine 601
Cysteine 553 and cysteine 574
Cysteine 680 and cysteine 707
Cysteine 680 and cysteine 715
Cysteine 652 and cysteine 678
Cysteine 594 and cysteine 619
Cysteine 619 and cysteine 646
Cysteine 574 and cysteine 577
Cysteine 691 and cysteine 707
Cysteine 659 and cysteine 691
Cysteine 678 and cysteine 691
Cysteine 619 and cysteine 622
Cysteine 601 and cysteine 646
Cysteine 558 and cysteine 577
A redox-regulated disulphide may form within Thrombospondin-2 between cysteines 577 and 588.

Details

Redox score ?
89
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
577
Residue number B
588
Peptide name
Thrombospondin-2

Ligandability

Cysteine 577 of Thrombospondin-2

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 588 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 622 and 646.

Details

Redox score ?
89
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
622
Residue number B
646
Peptide name
Thrombospondin-2

Ligandability

Cysteine 622 of Thrombospondin-2

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 646 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 558 and 574.

Details

Redox score ?
88
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
558
Residue number B
574
Peptide name
Thrombospondin-2

Ligandability

Cysteine 558 of Thrombospondin-2

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 574 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 553 and 564.

Details

Redox score ?
88
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
553
Residue number B
564
Peptide name
Thrombospondin-2

Ligandability

Cysteine 553 of Thrombospondin-2

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 564 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 659 and 678.

Details

Redox score ?
87
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
659
Residue number B
678
Peptide name
Thrombospondin-2

Ligandability

Cysteine 659 of Thrombospondin-2

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 678 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 652 and 665.

Details

Redox score ?
86
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
652
Residue number B
665
Peptide name
Thrombospondin-2

Ligandability

Cysteine 652 of Thrombospondin-2

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 665 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 594 and 610.

Details

Redox score ?
86
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
594
Residue number B
610
Peptide name
Thrombospondin-2

Ligandability

Cysteine 594 of Thrombospondin-2

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 610 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 680 and 691.

Details

Redox score ?
86
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
680
Residue number B
691
Peptide name
Thrombospondin-2

Ligandability

Cysteine 680 of Thrombospondin-2

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 691 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 707 and 715.

Details

Redox score ?
86
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
707
Residue number B
715
Peptide name
Thrombospondin-2

Ligandability

Cysteine 707 of Thrombospondin-2

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 715 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 601 and 619.

Details

Redox score ?
84
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
601
Residue number B
619
Peptide name
Thrombospondin-2

Ligandability

Cysteine 601 of Thrombospondin-2

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 619 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 912 and 932.

Details

Redox score ?
84
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
912
Residue number B
932
Peptide name
Thrombospondin-2

Ligandability

Cysteine 912 of Thrombospondin-2

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 932 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 838 and 858.

Details

Redox score ?
84
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
838
Residue number B
858
Peptide name
Thrombospondin-2

Ligandability

Cysteine 838 of Thrombospondin-2

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 858 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 876 and 896.

Details

Redox score ?
83
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
876
Residue number B
896
Peptide name
Thrombospondin-2

Ligandability

Cysteine 876 of Thrombospondin-2

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 896 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 779 and 799.

Details

Redox score ?
82
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
779
Residue number B
799
Peptide name
Thrombospondin-2

Ligandability

Cysteine 779 of Thrombospondin-2

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 799 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 948 and 1169.

Details

Redox score ?
82
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
948
Residue number B
1169
Peptide name
Thrombospondin-2

Ligandability

Cysteine 948 of Thrombospondin-2

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 1169 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 720 and 740.

Details

Redox score ?
82
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
720
Residue number B
740
Peptide name
Thrombospondin-2

Ligandability

Cysteine 720 of Thrombospondin-2

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 740 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 756 and 776.

Details

Redox score ?
81
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
756
Residue number B
776
Peptide name
Thrombospondin-2

Ligandability

Cysteine 756 of Thrombospondin-2

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 776 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 815 and 835.

Details

Redox score ?
81
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
815
Residue number B
835
Peptide name
Thrombospondin-2

Ligandability

Cysteine 815 of Thrombospondin-2

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 835 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 558 and 564.

Details

Redox score ?
77
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
558
Residue number B
564
Peptide name
Thrombospondin-2

Ligandability

Cysteine 558 of Thrombospondin-2

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 564 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 601 and 610.

Details

Redox score ?
74
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
601
Residue number B
610
Peptide name
Thrombospondin-2

Ligandability

Cysteine 601 of Thrombospondin-2

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 610 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 659 and 665.

Details

Redox score ?
73
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
659
Residue number B
665
Peptide name
Thrombospondin-2

Ligandability

Cysteine 659 of Thrombospondin-2

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 665 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 564 and 574.

Details

Redox score ?
67
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
564
Residue number B
574
Peptide name
Thrombospondin-2

Ligandability

Cysteine 564 of Thrombospondin-2

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 574 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 553 and 558.

Details

Redox score ?
66
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
553
Residue number B
558
Peptide name
Thrombospondin-2

Ligandability

Cysteine 553 of Thrombospondin-2

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 558 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 610 and 619.

Details

Redox score ?
66
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
5
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
610
Residue number B
619
Peptide name
Thrombospondin-2

Ligandability

Cysteine 610 of Thrombospondin-2

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 619 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 665 and 678.

Details

Redox score ?
65
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
665
Residue number B
678
Peptide name
Thrombospondin-2

Ligandability

Cysteine 665 of Thrombospondin-2

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 678 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 652 and 659.

Details

Redox score ?
63
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
652
Residue number B
659
Peptide name
Thrombospondin-2

Ligandability

Cysteine 652 of Thrombospondin-2

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 659 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 594 and 601.

Details

Redox score ?
62
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
594
Residue number B
601
Peptide name
Thrombospondin-2

Ligandability

Cysteine 594 of Thrombospondin-2

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 601 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 553 and 574. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
553
Residue number B
574
Peptide name
Thrombospondin-2

Ligandability

Cysteine 553 of Thrombospondin-2

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 574 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 680 and 707. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
680
Residue number B
707
Peptide name
Thrombospondin-2

Ligandability

Cysteine 680 of Thrombospondin-2

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 707 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 680 and 715. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
680
Residue number B
715
Peptide name
Thrombospondin-2

Ligandability

Cysteine 680 of Thrombospondin-2

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 715 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 652 and 678. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
652
Residue number B
678
Peptide name
Thrombospondin-2

Ligandability

Cysteine 652 of Thrombospondin-2

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 678 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 594 and 619. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
594
Residue number B
619
Peptide name
Thrombospondin-2

Ligandability

Cysteine 594 of Thrombospondin-2

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 619 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 619 and 646. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
619
Residue number B
646
Peptide name
Thrombospondin-2

Ligandability

Cysteine 619 of Thrombospondin-2

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 646 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 574 and 577. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
574
Residue number B
577
Peptide name
Thrombospondin-2

Ligandability

Cysteine 574 of Thrombospondin-2

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 577 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 691 and 707. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
691
Residue number B
707
Peptide name
Thrombospondin-2

Ligandability

Cysteine 691 of Thrombospondin-2

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 707 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 659 and 691. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
659
Residue number B
691
Peptide name
Thrombospondin-2

Ligandability

Cysteine 659 of Thrombospondin-2

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 691 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 678 and 691. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
678
Residue number B
691
Peptide name
Thrombospondin-2

Ligandability

Cysteine 678 of Thrombospondin-2

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 691 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 619 and 622. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
619
Residue number B
622
Peptide name
Thrombospondin-2

Ligandability

Cysteine 619 of Thrombospondin-2

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 622 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 601 and 646. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
601
Residue number B
646
Peptide name
Thrombospondin-2

Ligandability

Cysteine 601 of Thrombospondin-2

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 646 of Thrombospondin-2

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 Thrombospondin-2 between cysteines 558 and 577. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2rhp
Structure name
the thrombospondin-1 polymorphism asn700ser associated with cornoary artery disease causes local and long-ranging changes in protein structure
Structure deposition date
2007-10-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35442
Residue number A
558
Residue number B
577
Peptide name
Thrombospondin-2

Ligandability

Cysteine 558 of Thrombospondin-2

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 577 of Thrombospondin-2

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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