ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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CD226 antigen

Intramolecular
Cysteine 179 and cysteine 199
Cysteine 152 and cysteine 222
Cysteine 37 and cysteine 108
Cysteine 152 and cysteine 199
Cysteine 152 and cysteine 179
Cysteine 199 and cysteine 222
Cysteine 179 and cysteine 222
A redox-regulated disulphide may form within CD226 antigen between cysteines 179 and 199 (161 and 181 respectively in this structure).

Details

Redox score ?
85
PDB code
6isb
Structure name
crystal structure of human cd226
Structure deposition date
2018-11-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15762
Residue number A
179
Residue number B
199
Peptide name
CD226 antigen

Ligandability

Cysteine 179 of CD226 antigen

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 CD226 antigen

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 CD226 antigen between cysteines 152 and 222 (134 and 204 respectively in this structure).

Details

Redox score ?
84
PDB code
6isb
Structure name
crystal structure of human cd226
Structure deposition date
2018-11-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15762
Residue number A
152
Residue number B
222
Peptide name
CD226 antigen

Ligandability

Cysteine 152 of CD226 antigen

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 222 of CD226 antigen

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 CD226 antigen between cysteines 37 and 108.

Details

Redox score ?
82
PDB code
6o3o
Structure name
structure of human dnam-1 (cd226) bound to nectin-like protein-5 (necl-5)
Structure deposition date
2019-02-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15762
Residue number A
37
Residue number B
108
Peptide name
CD226 antigen

Ligandability

Cysteine 37 of CD226 antigen

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 108 of CD226 antigen

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 CD226 antigen between cysteines 152 and 199 (134 and 181 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
6isb
Structure name
crystal structure of human cd226
Structure deposition date
2018-11-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15762
Residue number A
152
Residue number B
199
Peptide name
CD226 antigen

Ligandability

Cysteine 152 of CD226 antigen

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 CD226 antigen

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 CD226 antigen between cysteines 152 and 179 (134 and 161 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
6isb
Structure name
crystal structure of human cd226
Structure deposition date
2018-11-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15762
Residue number A
152
Residue number B
179
Peptide name
CD226 antigen

Ligandability

Cysteine 152 of CD226 antigen

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 179 of CD226 antigen

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 CD226 antigen between cysteines 199 and 222 (181 and 204 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6isb
Structure name
crystal structure of human cd226
Structure deposition date
2018-11-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15762
Residue number A
199
Residue number B
222
Peptide name
CD226 antigen

Ligandability

Cysteine 199 of CD226 antigen

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 222 of CD226 antigen

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 CD226 antigen between cysteines 179 and 222 (161 and 204 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6isb
Structure name
crystal structure of human cd226
Structure deposition date
2018-11-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15762
Residue number A
179
Residue number B
222
Peptide name
CD226 antigen

Ligandability

Cysteine 179 of CD226 antigen

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 222 of CD226 antigen

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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