ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Vitamin D3 receptor

Intramolecular
Cysteine 60 and cysteine 66
Cysteine 60 and cysteine 76
Cysteine 60 and cysteine 79
Cysteine 24 and cysteine 27
Cysteine 66 and cysteine 79
Cysteine 76 and cysteine 79
Cysteine 66 and cysteine 76
Cysteine 27 and cysteine 41
Cysteine 27 and cysteine 44
Cysteine 24 and cysteine 44
More...
Cysteine 41 and cysteine 44
Cysteine 44 and cysteine 84
Cysteine 41 and cysteine 84
Cysteine 24 and cysteine 84
Cysteine 24 and cysteine 41
Cysteine 403 and cysteine 410
Cysteine 27 and cysteine 84
A redox-regulated disulphide may form within Vitamin D3 receptor between cysteines 60 and 66.

Details

Redox score ?
90
PDB code
1kb2
Structure name
crystal structure of vdr dna-binding domain bound to mouse osteopontin (spp) response element
Structure deposition date
2001-11-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
9
Peptide accession
P11473
Residue number A
60
Residue number B
66
Peptide name
Vitamin D3 receptor

Ligandability

Cysteine 60 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 66 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Vitamin D3 receptor between cysteines 60 and 76.

Details

Redox score ?
87
PDB code
1kb6
Structure name
crystal structure of vdr dna-binding domain bound to rat osteocalcin (oc) response element
Structure deposition date
2001-11-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
6
% buried
22
Peptide accession
P11473
Residue number A
60
Residue number B
76
Peptide name
Vitamin D3 receptor

Ligandability

Cysteine 60 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 76 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Vitamin D3 receptor between cysteines 60 and 79 (260 and 279 respectively in this structure).

Details

Redox score ?
86
PDB code
1kb6
Structure name
crystal structure of vdr dna-binding domain bound to rat osteocalcin (oc) response element
Structure deposition date
2001-11-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
6
% buried
0
Peptide accession
P11473
Residue number A
60
Residue number B
79
Peptide name
Vitamin D3 receptor

Ligandability

Cysteine 60 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 79 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Vitamin D3 receptor between cysteines 24 and 27.

Details

Redox score ?
85
PDB code
1kb6
Structure name
crystal structure of vdr dna-binding domain bound to rat osteocalcin (oc) response element
Structure deposition date
2001-11-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
5
% buried
nan
Peptide accession
P11473
Residue number A
24
Residue number B
27
Peptide name
Vitamin D3 receptor

Ligandability

Cysteine 24 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 27 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Vitamin D3 receptor between cysteines 66 and 79 (266 and 279 respectively in this structure).

Details

Redox score ?
84
PDB code
1kb2
Structure name
crystal structure of vdr dna-binding domain bound to mouse osteopontin (spp) response element
Structure deposition date
2001-11-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
7
% buried
0
Peptide accession
P11473
Residue number A
66
Residue number B
79
Peptide name
Vitamin D3 receptor

Ligandability

Cysteine 66 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 79 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Vitamin D3 receptor between cysteines 76 and 79 (276 and 279 respectively in this structure).

Details

Redox score ?
83
PDB code
1kb4
Structure name
crystal structure of vdr dna-binding domain bound to a canonical direct repeat with three base pair spacer (dr3) response element
Structure deposition date
2001-11-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
1
Peptide accession
P11473
Residue number A
76
Residue number B
79
Peptide name
Vitamin D3 receptor

Ligandability

Cysteine 76 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 79 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Vitamin D3 receptor between cysteines 66 and 76 (266 and 276 respectively in this structure).

Details

Redox score ?
81
PDB code
1kb2
Structure name
crystal structure of vdr dna-binding domain bound to mouse osteopontin (spp) response element
Structure deposition date
2001-11-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
2
Peptide accession
P11473
Residue number A
66
Residue number B
76
Peptide name
Vitamin D3 receptor

Ligandability

Cysteine 66 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 76 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Vitamin D3 receptor between cysteines 27 and 41 (227 and 241 respectively in this structure).

Details

Redox score ?
81
PDB code
1kb6
Structure name
crystal structure of vdr dna-binding domain bound to rat osteocalcin (oc) response element
Structure deposition date
2001-11-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
5
% buried
66
Peptide accession
P11473
Residue number A
27
Residue number B
41
Peptide name
Vitamin D3 receptor

Ligandability

Cysteine 27 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 41 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Vitamin D3 receptor between cysteines 27 and 44 (227 and 244 respectively in this structure).

Details

Redox score ?
81
PDB code
1kb2
Structure name
crystal structure of vdr dna-binding domain bound to mouse osteopontin (spp) response element
Structure deposition date
2001-11-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
5
% buried
64
Peptide accession
P11473
Residue number A
27
Residue number B
44
Peptide name
Vitamin D3 receptor

Ligandability

Cysteine 27 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 44 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Vitamin D3 receptor between cysteines 24 and 44.

Details

Redox score ?
65
PDB code
1kb6
Structure name
crystal structure of vdr dna-binding domain bound to rat osteocalcin (oc) response element
Structure deposition date
2001-11-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
15
% buried
nan
Peptide accession
P11473
Residue number A
24
Residue number B
44
Peptide name
Vitamin D3 receptor

Ligandability

Cysteine 24 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 44 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Vitamin D3 receptor between cysteines 41 and 44.

Details

Redox score ?
63
PDB code
1kb6
Structure name
crystal structure of vdr dna-binding domain bound to rat osteocalcin (oc) response element
Structure deposition date
2001-11-05
Thiol separation (Å)
3
Half-sphere exposure sum ?
71
Minimum pKa ?
15
% buried
84
Peptide accession
P11473
Residue number A
41
Residue number B
44
Peptide name
Vitamin D3 receptor

Ligandability

Cysteine 41 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 44 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Vitamin D3 receptor between cysteines 44 and 84 (244 and 284 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
1kb6
Structure name
crystal structure of vdr dna-binding domain bound to rat osteocalcin (oc) response element
Structure deposition date
2001-11-05
Thiol separation (Å)
6
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
86
Peptide accession
P11473
Residue number A
44
Residue number B
84
Peptide name
Vitamin D3 receptor

Ligandability

Cysteine 44 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 84 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Vitamin D3 receptor between cysteines 41 and 84. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
1kb2
Structure name
crystal structure of vdr dna-binding domain bound to mouse osteopontin (spp) response element
Structure deposition date
2001-11-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
5
% buried
88
Peptide accession
P11473
Residue number A
41
Residue number B
84
Peptide name
Vitamin D3 receptor

Ligandability

Cysteine 41 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 84 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Vitamin D3 receptor between cysteines 24 and 84. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
1kb6
Structure name
crystal structure of vdr dna-binding domain bound to rat osteocalcin (oc) response element
Structure deposition date
2001-11-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
12
% buried
nan
Peptide accession
P11473
Residue number A
24
Residue number B
84
Peptide name
Vitamin D3 receptor

Ligandability

Cysteine 24 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 84 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Vitamin D3 receptor between cysteines 24 and 41. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
1kb6
Structure name
crystal structure of vdr dna-binding domain bound to rat osteocalcin (oc) response element
Structure deposition date
2001-11-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
23
% buried
nan
Peptide accession
P11473
Residue number A
24
Residue number B
41
Peptide name
Vitamin D3 receptor

Ligandability

Cysteine 24 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 41 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Vitamin D3 receptor between cysteines 403 and 410. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
3az2
Structure name
crystal structure analysis of vitamin d receptor
Structure deposition date
2011-05-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
47
Minimum pKa ?
10
% buried
32
Peptide accession
P11473
Residue number A
403
Residue number B
410
Peptide name
Vitamin D3 receptor

Ligandability

Cysteine 403 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 410 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Vitamin D3 receptor between cysteines 27 and 84. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1kb4
Structure name
crystal structure of vdr dna-binding domain bound to a canonical direct repeat with three base pair spacer (dr3) response element
Structure deposition date
2001-11-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
nan
Peptide accession
P11473
Residue number A
27
Residue number B
84
Peptide name
Vitamin D3 receptor

Ligandability

Cysteine 27 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 84 of Vitamin D3 receptor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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