ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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CAD protein

Intramolecular
Cysteine 2016 and cysteine 2038
Cysteine 1636 and cysteine 1682
Cysteine 1613 and cysteine 1682
Cysteine 1613 and cysteine 1636
Cysteine 1501 and cysteine 1682
Cysteine 1501 and cysteine 1529 L
A redox-regulated disulphide may form within CAD protein between cysteines 2016 and 2038. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
5g1o
Structure name
aspartate transcarbamoylase domain of human cad in apo form
Structure deposition date
2016-03-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
86
Peptide accession
P27708
Residue number A
2016
Residue number B
2038
Peptide name
CAD protein

Ligandability

Cysteine 2016 of CAD protein

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 2038 of CAD protein

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 CAD protein between cysteines 1636 and 1682. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
4c6n
Structure name
crystal structure of the dihydroorotase domain of human cad e1637t mutant bound to substrate at ph 6
Structure deposition date
2013-09-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
P27708
Residue number A
1636
Residue number B
1682
Peptide name
CAD protein

Ligandability

Cysteine 1636 of CAD protein

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 1682 of CAD protein

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 CAD protein between cysteines 1613 and 1682. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4c6m
Structure name
crystal structure of the dihydroorotase domain of human cad bound to the inhibitor fluoroorotate at ph 7
Structure deposition date
2013-09-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
9
% buried
100
Peptide accession
P27708
Residue number A
1613
Residue number B
1682
Peptide name
CAD protein

Ligandability

Cysteine 1613 of CAD protein

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 1682 of CAD protein

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 CAD protein between cysteines 1613 and 1636. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
6hfn
Structure name
human dihydroorotase mutant f1563l co-crystallized with carbamoyl aspartate at ph 7
Structure deposition date
2018-08-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
89
Minimum pKa ?
9
% buried
100
Peptide accession
P27708
Residue number A
1613
Residue number B
1636
Peptide name
CAD protein

Ligandability

Cysteine 1613 of CAD protein

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 1636 of CAD protein

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 CAD protein between cysteines 1501 and 1682. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
4c6m
Structure name
crystal structure of the dihydroorotase domain of human cad bound to the inhibitor fluoroorotate at ph 7
Structure deposition date
2013-09-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
P27708
Residue number A
1501
Residue number B
1682
Peptide name
CAD protein

Ligandability

Cysteine 1501 of CAD protein

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 1682 of CAD protein

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 CAD protein between cysteines 1501 and 1529. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
23
PDB code
4c6i
Structure name
crystal structure of the dihydroorotase domain of human cad bound to substrate at ph 7
Structure deposition date
2013-09-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
98
Minimum pKa ?
12
% buried
100
Peptide accession
P27708
Residue number A
1501
Residue number B
1529
Peptide name
CAD protein

Ligandability

Cysteine 1501 of CAD protein

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 1529 of CAD protein

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.

Ligandable in the dataset of Kuljanin et al.

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