ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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C-type lectin domain family 4 member D

Intermolecular
Cysteine 66 and cysteine 66
Cysteine 66 and cysteine 83
Cysteine 83 and cysteine 83
Intramolecular
Cysteine 182 and cysteine 199
Cysteine 112 and cysteine 207
Cysteine 84 and cysteine 95
Cysteine 83 and cysteine 84
Cysteine 83 and cysteine 95
Cysteine 66 and cysteine 84
Cysteine 66 and cysteine 95
A redox-regulated disulphide may form between two units of C-type lectin domain family 4 member D at cysteines 66 and 66.

Details

Redox score ?
71
PDB code
3whd
Structure name
c-type lectin, human mcl
Structure deposition date
2013-08-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide A name
C-type lectin domain family 4 member D
Peptide B name
C-type lectin domain family 4 member D
Peptide A accession
Q8WXI8
Peptide B accession
Q8WXI8
Peptide A residue number
66
Peptide B residue number
66

Ligandability

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 between two units of C-type lectin domain family 4 member D at cysteines 66 and 83.

Details

Redox score ?
62
PDB code
3whd
Structure name
c-type lectin, human mcl
Structure deposition date
2013-08-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide A name
C-type lectin domain family 4 member D
Peptide B name
C-type lectin domain family 4 member D
Peptide A accession
Q8WXI8
Peptide B accession
Q8WXI8
Peptide A residue number
66
Peptide B residue number
83

Ligandability

Cysteine 66 of C-type lectin domain family 4 member D

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 83 of C-type lectin domain family 4 member D

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 between two units of C-type lectin domain family 4 member D at cysteines 83 and 83. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
3whd
Structure name
c-type lectin, human mcl
Structure deposition date
2013-08-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide A name
C-type lectin domain family 4 member D
Peptide B name
C-type lectin domain family 4 member D
Peptide A accession
Q8WXI8
Peptide B accession
Q8WXI8
Peptide A residue number
83
Peptide B residue number
83

Ligandability

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 C-type lectin domain family 4 member D between cysteines 182 and 199.

Details

Redox score ?
82
PDB code
3whd
Structure name
c-type lectin, human mcl
Structure deposition date
2013-08-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8WXI8
Residue number A
182
Residue number B
199
Peptide name
C-type lectin domain family 4 member D

Ligandability

Cysteine 182 of C-type lectin domain family 4 member D

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 199 of C-type lectin domain family 4 member D

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 C-type lectin domain family 4 member D between cysteines 112 and 207.

Details

Redox score ?
81
PDB code
3whd
Structure name
c-type lectin, human mcl
Structure deposition date
2013-08-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8WXI8
Residue number A
112
Residue number B
207
Peptide name
C-type lectin domain family 4 member D

Ligandability

Cysteine 112 of C-type lectin domain family 4 member D

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 207 of C-type lectin domain family 4 member D

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 C-type lectin domain family 4 member D between cysteines 84 and 95.

Details

Redox score ?
79
PDB code
3whd
Structure name
c-type lectin, human mcl
Structure deposition date
2013-08-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8WXI8
Residue number A
84
Residue number B
95
Peptide name
C-type lectin domain family 4 member D

Ligandability

Cysteine 84 of C-type lectin domain family 4 member D

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 95 of C-type lectin domain family 4 member D

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 C-type lectin domain family 4 member D between cysteines 83 and 84. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
3whd
Structure name
c-type lectin, human mcl
Structure deposition date
2013-08-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8WXI8
Residue number A
83
Residue number B
84
Peptide name
C-type lectin domain family 4 member D

Ligandability

Cysteine 83 of C-type lectin domain family 4 member D

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 C-type lectin domain family 4 member D

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 C-type lectin domain family 4 member D between cysteines 83 and 95. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
3whd
Structure name
c-type lectin, human mcl
Structure deposition date
2013-08-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8WXI8
Residue number A
83
Residue number B
95
Peptide name
C-type lectin domain family 4 member D

Ligandability

Cysteine 83 of C-type lectin domain family 4 member D

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 95 of C-type lectin domain family 4 member D

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 C-type lectin domain family 4 member D between cysteines 66 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
3whd
Structure name
c-type lectin, human mcl
Structure deposition date
2013-08-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8WXI8
Residue number A
66
Residue number B
84
Peptide name
C-type lectin domain family 4 member D

Ligandability

Cysteine 66 of C-type lectin domain family 4 member D

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 C-type lectin domain family 4 member D

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 C-type lectin domain family 4 member D between cysteines 66 and 95. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
3whd
Structure name
c-type lectin, human mcl
Structure deposition date
2013-08-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8WXI8
Residue number A
66
Residue number B
95
Peptide name
C-type lectin domain family 4 member D

Ligandability

Cysteine 66 of C-type lectin domain family 4 member D

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 95 of C-type lectin domain family 4 member D

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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