ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Lectin-related NK cell receptor LY49L4

Intermolecular
Cysteine 107 and cysteine 107
Cysteine 148 and cysteine 148
Cysteine 153 and cysteine 148
Cysteine 153 and cysteine 153
Intramolecular
Cysteine 235 and cysteine 248
Cysteine 170 and cysteine 256
Cysteine 166 and cysteine 254
Cysteine 166 and cysteine 170
Cysteine 170 and cysteine 254
Cysteine 254 and cysteine 256
More...
Cysteine 166 and cysteine 256
Cysteine 166 and cysteine 235
A redox-regulated disulphide may form between two units of Lectin-related NK cell receptor LY49L4 at cysteines 107 and 107.

Details

Redox score ?
89
PDB code
3g8l
Structure name
crystal structure of murine natural killer cell receptor, ly49l4
Structure deposition date
2009-02-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
36
Minimum pKa ?
nan
% buried
nan
Peptide A name
Lectin-related NK cell receptor LY49L4
Peptide B name
Lectin-related NK cell receptor LY49L4
Peptide A accession
Q9JIP9
Peptide B accession
Q9JIP9
Peptide A residue number
107
Peptide B residue number
107

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 Lectin-related NK cell receptor LY49L4 at cysteines 148 and 148.

Details

Redox score ?
63
PDB code
3g8l
Structure name
crystal structure of murine natural killer cell receptor, ly49l4
Structure deposition date
2009-02-12
Thiol separation (Å)
5
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide A name
Lectin-related NK cell receptor LY49L4
Peptide B name
Lectin-related NK cell receptor LY49L4
Peptide A accession
Q9JIP9
Peptide B accession
Q9JIP9
Peptide A residue number
148
Peptide B residue number
148

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 Lectin-related NK cell receptor LY49L4 at cysteines 153 and 148.

Details

Redox score ?
60
PDB code
3g8l
Structure name
crystal structure of murine natural killer cell receptor, ly49l4
Structure deposition date
2009-02-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide A name
Lectin-related NK cell receptor LY49L4
Peptide B name
Lectin-related NK cell receptor LY49L4
Peptide A accession
Q9JIP9
Peptide B accession
Q9JIP9
Peptide A residue number
153
Peptide B residue number
148

Ligandability

Cysteine 153 of Lectin-related NK cell receptor LY49L4

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 148 of Lectin-related NK cell receptor LY49L4

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 Lectin-related NK cell receptor LY49L4 at cysteines 153 and 153. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
3g8l
Structure name
crystal structure of murine natural killer cell receptor, ly49l4
Structure deposition date
2009-02-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide A name
Lectin-related NK cell receptor LY49L4
Peptide B name
Lectin-related NK cell receptor LY49L4
Peptide A accession
Q9JIP9
Peptide B accession
Q9JIP9
Peptide A residue number
153
Peptide B residue number
153

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 Lectin-related NK cell receptor LY49L4 between cysteines 235 and 248.

Details

Redox score ?
83
PDB code
3g8k
Structure name
crystal structure of murine natural killer cell receptor, ly49l4
Structure deposition date
2009-02-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9JIP9
Residue number A
235
Residue number B
248
Peptide name
Lectin-related NK cell receptor LY49L4

Ligandability

Cysteine 235 of Lectin-related NK cell receptor LY49L4

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 248 of Lectin-related NK cell receptor LY49L4

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 LY49L4 between cysteines 170 and 256.

Details

Redox score ?
82
PDB code
3g8l
Structure name
crystal structure of murine natural killer cell receptor, ly49l4
Structure deposition date
2009-02-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9JIP9
Residue number A
170
Residue number B
256
Peptide name
Lectin-related NK cell receptor LY49L4

Ligandability

Cysteine 170 of Lectin-related NK cell receptor LY49L4

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 256 of Lectin-related NK cell receptor LY49L4

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 LY49L4 between cysteines 166 and 254.

Details

Redox score ?
81
PDB code
3g8k
Structure name
crystal structure of murine natural killer cell receptor, ly49l4
Structure deposition date
2009-02-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9JIP9
Residue number A
166
Residue number B
254
Peptide name
Lectin-related NK cell receptor LY49L4

Ligandability

Cysteine 166 of Lectin-related NK cell receptor LY49L4

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 254 of Lectin-related NK cell receptor LY49L4

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 LY49L4 between cysteines 166 and 170.

Details

Redox score ?
61
PDB code
3g8l
Structure name
crystal structure of murine natural killer cell receptor, ly49l4
Structure deposition date
2009-02-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9JIP9
Residue number A
166
Residue number B
170
Peptide name
Lectin-related NK cell receptor LY49L4

Ligandability

Cysteine 166 of Lectin-related NK cell receptor LY49L4

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 170 of Lectin-related NK cell receptor LY49L4

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 LY49L4 between cysteines 170 and 254. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
60
PDB code
3g8l
Structure name
crystal structure of murine natural killer cell receptor, ly49l4
Structure deposition date
2009-02-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9JIP9
Residue number A
170
Residue number B
254
Peptide name
Lectin-related NK cell receptor LY49L4

Ligandability

Cysteine 170 of Lectin-related NK cell receptor LY49L4

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 254 of Lectin-related NK cell receptor LY49L4

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 LY49L4 between cysteines 254 and 256. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
3g8l
Structure name
crystal structure of murine natural killer cell receptor, ly49l4
Structure deposition date
2009-02-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9JIP9
Residue number A
254
Residue number B
256
Peptide name
Lectin-related NK cell receptor LY49L4

Ligandability

Cysteine 254 of Lectin-related NK cell receptor LY49L4

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 256 of Lectin-related NK cell receptor LY49L4

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 LY49L4 between cysteines 166 and 256. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
3g8l
Structure name
crystal structure of murine natural killer cell receptor, ly49l4
Structure deposition date
2009-02-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9JIP9
Residue number A
166
Residue number B
256
Peptide name
Lectin-related NK cell receptor LY49L4

Ligandability

Cysteine 166 of Lectin-related NK cell receptor LY49L4

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 256 of Lectin-related NK cell receptor LY49L4

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 LY49L4 between cysteines 166 and 235. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3g8k
Structure name
crystal structure of murine natural killer cell receptor, ly49l4
Structure deposition date
2009-02-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9JIP9
Residue number A
166
Residue number B
235
Peptide name
Lectin-related NK cell receptor LY49L4

Ligandability

Cysteine 166 of Lectin-related NK cell receptor LY49L4

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 235 of Lectin-related NK cell receptor LY49L4

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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