ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Prostaglandin-H2 D-isomerase

Intermolecular
Cysteine 89 and cysteine 89
Cysteine 89 and cysteine 186
Intramolecular
Cysteine 65 and cysteine 89
A redox-regulated disulphide may form between two units of Prostaglandin-H2 D-isomerase at cysteines 89 and 89. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
4ory
Structure name
three-dimensional structure of the c65a-k59a double mutant of human lipocalin-type prostaglandin d synthase holo, second crystal form
Structure deposition date
2014-02-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide A name
Prostaglandin-H2 D-isomerase
Peptide B name
Prostaglandin-H2 D-isomerase
Peptide A accession
P41222
Peptide B accession
P41222
Peptide A residue number
89
Peptide B residue number
89

Ligandability

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 Prostaglandin-H2 D-isomerase at cysteines 89 and 186. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4ory
Structure name
three-dimensional structure of the c65a-k59a double mutant of human lipocalin-type prostaglandin d synthase holo, second crystal form
Structure deposition date
2014-02-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide A name
Prostaglandin-H2 D-isomerase
Peptide B name
Prostaglandin-H2 D-isomerase
Peptide A accession
P41222
Peptide B accession
P41222
Peptide A residue number
89
Peptide B residue number
186

Ligandability

Cysteine 89 of Prostaglandin-H2 D-isomerase

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 186 of Prostaglandin-H2 D-isomerase

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 Prostaglandin-H2 D-isomerase between cysteines 65 and 89.

Details

Redox score ?
74
PDB code
5wy9
Structure name
apo form crystal structure of human lipocalin pgds
Structure deposition date
2017-01-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
6
Peptide accession
P41222
Residue number A
65
Residue number B
89
Peptide name
Prostaglandin-H2 D-isomerase

Ligandability

Cysteine 65 of Prostaglandin-H2 D-isomerase

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 89 of Prostaglandin-H2 D-isomerase

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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