ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ornithine decarboxylase

Intermolecular
Cysteine 164 and cysteine 360 L
Cysteine 360 and cysteine 70 L
Cysteine 360 and cysteine 114 L
A redox-regulated disulphide may form between two units of Ornithine decarboxylase at cysteines 164 and 360. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
2oo0
Structure name
a structural insight into the inhibition of human and leishmania donovani ornithine decarboxylases by 3-aminooxy-1-aminopropane
Structure deposition date
2007-01-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
9
% buried
97
Peptide A name
Ornithine decarboxylase
Peptide B name
Ornithine decarboxylase
Peptide A accession
P11926
Peptide B accession
P11926
Peptide A residue number
164
Peptide B residue number
360

Ligandability

Cysteine 164 of Ornithine decarboxylase

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 360 of Ornithine decarboxylase

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.

A redox-regulated disulphide may form between two units of Ornithine decarboxylase at cysteines 360 and 70. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
2oo0
Structure name
a structural insight into the inhibition of human and leishmania donovani ornithine decarboxylases by 3-aminooxy-1-aminopropane
Structure deposition date
2007-01-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
90
Minimum pKa ?
9
% buried
100
Peptide A name
Ornithine decarboxylase
Peptide B name
Ornithine decarboxylase
Peptide A accession
P11926
Peptide B accession
P11926
Peptide A residue number
360
Peptide B residue number
70

Ligandability

Cysteine 360 of Ornithine decarboxylase

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.

Cysteine 70 of Ornithine decarboxylase

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 between two units of Ornithine decarboxylase at cysteines 360 and 114. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
1d7k
Structure name
crystal structure of human ornithine decarboxylase at 2
Structure deposition date
1999-10-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
100
Peptide A name
Ornithine decarboxylase
Peptide B name
Ornithine decarboxylase
Peptide A accession
P11926
Peptide B accession
P11926
Peptide A residue number
360
Peptide B residue number
114

Ligandability

Cysteine 360 of Ornithine decarboxylase

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.

Cysteine 114 of Ornithine decarboxylase

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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