ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Lectin-related NK cell receptor LY49G1

Intramolecular
Cysteine 163 and cysteine 168
Cysteine 185 and cysteine 271
Cysteine 181 and cysteine 269
Cysteine 185 and cysteine 269
Cysteine 181 and cysteine 185
Cysteine 269 and cysteine 271
Cysteine 181 and cysteine 271
Cysteine 181 and cysteine 250
A redox-regulated disulphide may form within Lectin-related NK cell receptor LY49G1 between cysteines 163 and 168 (145 and 150 respectively in this structure).

Details

Redox score ?
82
PDB code
3cad
Structure name
crystal structure of natural killer cell receptor, ly49g
Structure deposition date
2008-02-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9JHV6
Residue number A
163
Residue number B
168
Peptide name
Lectin-related NK cell receptor LY49G1

Ligandability

Cysteine 163 of Lectin-related NK cell receptor LY49G1

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 168 of Lectin-related NK cell receptor LY49G1

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 Lectin-related NK cell receptor LY49G1 between cysteines 185 and 271 (167 and 253 respectively in this structure).

Details

Redox score ?
82
PDB code
3cad
Structure name
crystal structure of natural killer cell receptor, ly49g
Structure deposition date
2008-02-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9JHV6
Residue number A
185
Residue number B
271
Peptide name
Lectin-related NK cell receptor LY49G1

Ligandability

Cysteine 185 of Lectin-related NK cell receptor LY49G1

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 271 of Lectin-related NK cell receptor LY49G1

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 Lectin-related NK cell receptor LY49G1 between cysteines 181 and 269 (163 and 251 respectively in this structure).

Details

Redox score ?
82
PDB code
3cad
Structure name
crystal structure of natural killer cell receptor, ly49g
Structure deposition date
2008-02-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9JHV6
Residue number A
181
Residue number B
269
Peptide name
Lectin-related NK cell receptor LY49G1

Ligandability

Cysteine 181 of Lectin-related NK cell receptor LY49G1

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 269 of Lectin-related NK cell receptor LY49G1

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 Lectin-related NK cell receptor LY49G1 between cysteines 185 and 269 (167 and 251 respectively in this structure).

Details

Redox score ?
64
PDB code
3cad
Structure name
crystal structure of natural killer cell receptor, ly49g
Structure deposition date
2008-02-19
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9JHV6
Residue number A
185
Residue number B
269
Peptide name
Lectin-related NK cell receptor LY49G1

Ligandability

Cysteine 185 of Lectin-related NK cell receptor LY49G1

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 269 of Lectin-related NK cell receptor LY49G1

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 Lectin-related NK cell receptor LY49G1 between cysteines 181 and 185 (163 and 167 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
3cad
Structure name
crystal structure of natural killer cell receptor, ly49g
Structure deposition date
2008-02-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9JHV6
Residue number A
181
Residue number B
185
Peptide name
Lectin-related NK cell receptor LY49G1

Ligandability

Cysteine 181 of Lectin-related NK cell receptor LY49G1

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 185 of Lectin-related NK cell receptor LY49G1

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 Lectin-related NK cell receptor LY49G1 between cysteines 269 and 271 (251 and 253 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
3cad
Structure name
crystal structure of natural killer cell receptor, ly49g
Structure deposition date
2008-02-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9JHV6
Residue number A
269
Residue number B
271
Peptide name
Lectin-related NK cell receptor LY49G1

Ligandability

Cysteine 269 of Lectin-related NK cell receptor LY49G1

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 271 of Lectin-related NK cell receptor LY49G1

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 Lectin-related NK cell receptor LY49G1 between cysteines 181 and 271 (163 and 253 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
3cad
Structure name
crystal structure of natural killer cell receptor, ly49g
Structure deposition date
2008-02-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9JHV6
Residue number A
181
Residue number B
271
Peptide name
Lectin-related NK cell receptor LY49G1

Ligandability

Cysteine 181 of Lectin-related NK cell receptor LY49G1

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 271 of Lectin-related NK cell receptor LY49G1

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 Lectin-related NK cell receptor LY49G1 between cysteines 181 and 250 (163 and 232 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
3cad
Structure name
crystal structure of natural killer cell receptor, ly49g
Structure deposition date
2008-02-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9JHV6
Residue number A
181
Residue number B
250
Peptide name
Lectin-related NK cell receptor LY49G1

Ligandability

Cysteine 181 of Lectin-related NK cell receptor LY49G1

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 250 of Lectin-related NK cell receptor LY49G1

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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