ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Protein odd-skipped-related 2

Intramolecular
Cysteine 202 and cysteine 205
Cysteine 174 and cysteine 177
Cysteine 230 and cysteine 233
Cysteine 205 and cysteine 233
Cysteine 205 and cysteine 238
A redox-regulated disulphide may form within Protein odd-skipped-related 2 between cysteines 202 and 205 (48 and 51 respectively in this structure).

Details

Redox score ?
88
PDB code
2ee8
Structure name
solution structure of three zf-c2h2 domains from mouse protein odd- skipped-related 2 splicing isoform 2
Structure deposition date
2007-02-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
7
% buried
0
Peptide accession
Q91ZD1
Residue number A
202
Residue number B
205
Peptide name
Protein odd-skipped-related 2

Ligandability

Cysteine 202 of Protein odd-skipped-related 2

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 205 of Protein odd-skipped-related 2

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 Protein odd-skipped-related 2 between cysteines 174 and 177 (20 and 23 respectively in this structure).

Details

Redox score ?
87
PDB code
2ee8
Structure name
solution structure of three zf-c2h2 domains from mouse protein odd- skipped-related 2 splicing isoform 2
Structure deposition date
2007-02-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
6
% buried
0
Peptide accession
Q91ZD1
Residue number A
174
Residue number B
177
Peptide name
Protein odd-skipped-related 2

Ligandability

Cysteine 174 of Protein odd-skipped-related 2

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 177 of Protein odd-skipped-related 2

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 Protein odd-skipped-related 2 between cysteines 230 and 233 (76 and 79 respectively in this structure).

Details

Redox score ?
87
PDB code
2ee8
Structure name
solution structure of three zf-c2h2 domains from mouse protein odd- skipped-related 2 splicing isoform 2
Structure deposition date
2007-02-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
6
% buried
0
Peptide accession
Q91ZD1
Residue number A
230
Residue number B
233
Peptide name
Protein odd-skipped-related 2

Ligandability

Cysteine 230 of Protein odd-skipped-related 2

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 233 of Protein odd-skipped-related 2

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 Protein odd-skipped-related 2 between cysteines 205 and 233 (51 and 79 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2ee8
Structure name
solution structure of three zf-c2h2 domains from mouse protein odd- skipped-related 2 splicing isoform 2
Structure deposition date
2007-02-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
28
Minimum pKa ?
9
% buried
0
Peptide accession
Q91ZD1
Residue number A
205
Residue number B
233
Peptide name
Protein odd-skipped-related 2

Ligandability

Cysteine 205 of Protein odd-skipped-related 2

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 233 of Protein odd-skipped-related 2

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 Protein odd-skipped-related 2 between cysteines 205 and 238 (51 and 84 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
2ee8
Structure name
solution structure of three zf-c2h2 domains from mouse protein odd- skipped-related 2 splicing isoform 2
Structure deposition date
2007-02-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
28
Minimum pKa ?
9
% buried
0
Peptide accession
Q91ZD1
Residue number A
205
Residue number B
238
Peptide name
Protein odd-skipped-related 2

Ligandability

Cysteine 205 of Protein odd-skipped-related 2

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 238 of Protein odd-skipped-related 2

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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