ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Protein N-terminal glutamine amidohydrolase

Intramolecular
Cysteine 26 and cysteine 28
Cysteine 36 and cysteine 50
Cysteine 36 and cysteine 21
Cysteine 50 and cysteine 21
A redox-regulated disulphide may form within Protein N-terminal glutamine amidohydrolase between cysteines 26 and 28. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
3c9q
Structure name
crystal structure of the uncharacterized human protein c8orf32 with bound peptide
Structure deposition date
2008-02-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
75
Peptide accession
Q96HA8
Residue number A
26
Residue number B
28
Peptide name
Protein N-terminal glutamine amidohydrolase

Ligandability

Cysteine 26 of Protein N-terminal glutamine amidohydrolase

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 28 of Protein N-terminal glutamine amidohydrolase

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 N-terminal glutamine amidohydrolase between cysteines 36 and 50. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
6kgj
Structure name
m1q-hntaq1 c28s
Structure deposition date
2019-07-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
89
Peptide accession
Q96HA8
Residue number A
36
Residue number B
50
Peptide name
Protein N-terminal glutamine amidohydrolase

Ligandability

Cysteine 36 of Protein N-terminal glutamine amidohydrolase

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 50 of Protein N-terminal glutamine amidohydrolase

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 N-terminal glutamine amidohydrolase between cysteines 36 and 21 (36 and 134 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6kgj
Structure name
m1q-hntaq1 c28s
Structure deposition date
2019-07-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
69
Peptide accession
Q96HA8
Residue number A
36
Residue number B
21
Peptide name
Protein N-terminal glutamine amidohydrolase

Ligandability

Cysteine 36 of Protein N-terminal glutamine amidohydrolase

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 21 of Protein N-terminal glutamine amidohydrolase

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.

Uncertain whether structure cysteine 134 has been assigned to correct residue.
A redox-regulated disulphide may form within Protein N-terminal glutamine amidohydrolase between cysteines 50 and 21 (50 and 134 respectively in this structure).

Details

Redox score ?
nan
PDB code
6kgj
Structure name
m1q-hntaq1 c28s
Structure deposition date
2019-07-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
57
Peptide accession
Q96HA8
Residue number A
50
Residue number B
21
Peptide name
Protein N-terminal glutamine amidohydrolase

Ligandability

Cysteine 50 of Protein N-terminal glutamine amidohydrolase

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 21 of Protein N-terminal glutamine amidohydrolase

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.

Uncertain whether structure cysteine 134 has been assigned to correct residue.
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