ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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UL16-binding protein 3

Intramolecular
Cysteine 51 and cysteine 67
Cysteine 128 and cysteine 191
Cysteine 128 and cysteine 130 L
Cysteine 130 and cysteine 191 L
A redox-regulated disulphide may form within UL16-binding protein 3 between cysteines 51 and 67 (30 and 46 respectively in this structure).

Details

Redox score ?
82
PDB code
1kcg
Structure name
nkg2d in complex with ulbp3
Structure deposition date
2001-11-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZM4
Residue number A
51
Residue number B
67
Peptide name
UL16-binding protein 3

Ligandability

Cysteine 51 of UL16-binding protein 3

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 67 of UL16-binding protein 3

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 UL16-binding protein 3 between cysteines 128 and 191 (107 and 170 respectively in this structure).

Details

Redox score ?
80
PDB code
1kcg
Structure name
nkg2d in complex with ulbp3
Structure deposition date
2001-11-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZM4
Residue number A
128
Residue number B
191
Peptide name
UL16-binding protein 3

Ligandability

Cysteine 128 of UL16-binding protein 3

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 191 of UL16-binding protein 3

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 UL16-binding protein 3 between cysteines 128 and 130 (107 and 109 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
1kcg
Structure name
nkg2d in complex with ulbp3
Structure deposition date
2001-11-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZM4
Residue number A
128
Residue number B
130
Peptide name
UL16-binding protein 3

Ligandability

Cysteine 128 of UL16-binding protein 3

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 130 of UL16-binding protein 3

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.

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 UL16-binding protein 3 between cysteines 130 and 191 (109 and 170 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
1kcg
Structure name
nkg2d in complex with ulbp3
Structure deposition date
2001-11-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZM4
Residue number A
130
Residue number B
191
Peptide name
UL16-binding protein 3

Ligandability

Cysteine 130 of UL16-binding protein 3

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.

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 191 of UL16-binding protein 3

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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