ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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C-type lectin domain family 6 member A

Intramolecular
Cysteine 66 and cysteine 78
Cysteine 107 and cysteine 202
Cysteine 79 and cysteine 90
Cysteine 176 and cysteine 194
Cysteine 78 and cysteine 79
Cysteine 66 and cysteine 79
Cysteine 78 and cysteine 90
Cysteine 66 and cysteine 90
A redox-regulated disulphide may form within C-type lectin domain family 6 member A between cysteines 66 and 78.

Details

Redox score ?
84
PDB code
5vyb
Structure name
structure of the carbohydrate recognition domain of dectin-2 complexed with a mammalian-type high mannose man9glcnac2 oligosaccharide
Structure deposition date
2017-05-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6EIG7
Residue number A
66
Residue number B
78
Peptide name
C-type lectin domain family 6 member A

Ligandability

Cysteine 66 of C-type lectin domain family 6 member A

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 78 of C-type lectin domain family 6 member A

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 6 member A between cysteines 107 and 202.

Details

Redox score ?
82
PDB code
5vyb
Structure name
structure of the carbohydrate recognition domain of dectin-2 complexed with a mammalian-type high mannose man9glcnac2 oligosaccharide
Structure deposition date
2017-05-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6EIG7
Residue number A
107
Residue number B
202
Peptide name
C-type lectin domain family 6 member A

Ligandability

Cysteine 107 of C-type lectin domain family 6 member A

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 202 of C-type lectin domain family 6 member A

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 6 member A between cysteines 79 and 90.

Details

Redox score ?
82
PDB code
5vyb
Structure name
structure of the carbohydrate recognition domain of dectin-2 complexed with a mammalian-type high mannose man9glcnac2 oligosaccharide
Structure deposition date
2017-05-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6EIG7
Residue number A
79
Residue number B
90
Peptide name
C-type lectin domain family 6 member A

Ligandability

Cysteine 79 of C-type lectin domain family 6 member A

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 90 of C-type lectin domain family 6 member A

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 6 member A between cysteines 176 and 194.

Details

Redox score ?
81
PDB code
5vyb
Structure name
structure of the carbohydrate recognition domain of dectin-2 complexed with a mammalian-type high mannose man9glcnac2 oligosaccharide
Structure deposition date
2017-05-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6EIG7
Residue number A
176
Residue number B
194
Peptide name
C-type lectin domain family 6 member A

Ligandability

Cysteine 176 of C-type lectin domain family 6 member A

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 194 of C-type lectin domain family 6 member A

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 6 member A between cysteines 78 and 79. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
5vyb
Structure name
structure of the carbohydrate recognition domain of dectin-2 complexed with a mammalian-type high mannose man9glcnac2 oligosaccharide
Structure deposition date
2017-05-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6EIG7
Residue number A
78
Residue number B
79
Peptide name
C-type lectin domain family 6 member A

Ligandability

Cysteine 78 of C-type lectin domain family 6 member A

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 C-type lectin domain family 6 member A

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 6 member A between cysteines 66 and 79. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
5vyb
Structure name
structure of the carbohydrate recognition domain of dectin-2 complexed with a mammalian-type high mannose man9glcnac2 oligosaccharide
Structure deposition date
2017-05-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6EIG7
Residue number A
66
Residue number B
79
Peptide name
C-type lectin domain family 6 member A

Ligandability

Cysteine 66 of C-type lectin domain family 6 member A

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 C-type lectin domain family 6 member A

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 6 member A between cysteines 78 and 90. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
5vyb
Structure name
structure of the carbohydrate recognition domain of dectin-2 complexed with a mammalian-type high mannose man9glcnac2 oligosaccharide
Structure deposition date
2017-05-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6EIG7
Residue number A
78
Residue number B
90
Peptide name
C-type lectin domain family 6 member A

Ligandability

Cysteine 78 of C-type lectin domain family 6 member A

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 90 of C-type lectin domain family 6 member A

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 6 member A between cysteines 66 and 90. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5vyb
Structure name
structure of the carbohydrate recognition domain of dectin-2 complexed with a mammalian-type high mannose man9glcnac2 oligosaccharide
Structure deposition date
2017-05-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6EIG7
Residue number A
66
Residue number B
90
Peptide name
C-type lectin domain family 6 member A

Ligandability

Cysteine 66 of C-type lectin domain family 6 member A

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 90 of C-type lectin domain family 6 member A

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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