ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Prolyl 4-hydroxylase subunit alpha-2

Intermolecular
Cysteine 529 and cysteine 53 of Protein disulfide-isomerase L
Cysteine 311 and cysteine 397 of Protein disulfide-isomerase L
Cysteine 529 and cysteine 56 of Protein disulfide-isomerase
Cysteine 311 and cysteine 400 of Protein disulfide-isomerase L
A redox-regulated disulphide may form between cysteine 529 of Prolyl 4-hydroxylase subunit alpha-2 and cysteine 53 of Protein disulfide-isomerase.

Details

Redox score ?
86
PDB code
7zsc
Structure name
crystal structure of the heterodimeric human c-p4h-ii with truncated alpha subunit (c-p4h-ii delta281)
Structure deposition date
2022-05-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide A name
Prolyl 4-hydroxylase subunit alpha-2
Peptide B name
Protein disulfide-isomerase
Peptide A accession
O15460
Peptide B accession
P07237
Peptide A residue number
529
Peptide B residue number
53

Ligandability

Cysteine 529 of Prolyl 4-hydroxylase subunit alpha-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 53 of Protein disulfide-isomerase

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

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 cysteine 311 of Prolyl 4-hydroxylase subunit alpha-2 and cysteine 397 of Protein disulfide-isomerase.

Details

Redox score ?
85
PDB code
7zsc
Structure name
crystal structure of the heterodimeric human c-p4h-ii with truncated alpha subunit (c-p4h-ii delta281)
Structure deposition date
2022-05-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide A name
Prolyl 4-hydroxylase subunit alpha-2
Peptide B name
Protein disulfide-isomerase
Peptide A accession
O15460
Peptide B accession
P07237
Peptide A residue number
311
Peptide B residue number
397

Ligandability

Cysteine 311 of Prolyl 4-hydroxylase subunit alpha-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 397 of Protein disulfide-isomerase

Not ligandable in the dataset of Yang et al.

Ligandable in the dataset of Yan et al.

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 cysteine 529 of Prolyl 4-hydroxylase subunit alpha-2 and cysteine 56 of Protein disulfide-isomerase. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
7zsc
Structure name
crystal structure of the heterodimeric human c-p4h-ii with truncated alpha subunit (c-p4h-ii delta281)
Structure deposition date
2022-05-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
13
% buried
nan
Peptide A name
Prolyl 4-hydroxylase subunit alpha-2
Peptide B name
Protein disulfide-isomerase
Peptide A accession
O15460
Peptide B accession
P07237
Peptide A residue number
529
Peptide B residue number
56

Ligandability

Cysteine 529 of Prolyl 4-hydroxylase subunit alpha-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 56 of Protein disulfide-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 between cysteine 311 of Prolyl 4-hydroxylase subunit alpha-2 and cysteine 400 of Protein disulfide-isomerase. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
7zsc
Structure name
crystal structure of the heterodimeric human c-p4h-ii with truncated alpha subunit (c-p4h-ii delta281)
Structure deposition date
2022-05-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
13
% buried
nan
Peptide A name
Prolyl 4-hydroxylase subunit alpha-2
Peptide B name
Protein disulfide-isomerase
Peptide A accession
O15460
Peptide B accession
P07237
Peptide A residue number
311
Peptide B residue number
400

Ligandability

Cysteine 311 of Prolyl 4-hydroxylase subunit alpha-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 400 of Protein disulfide-isomerase

Not ligandable in the dataset of Yang et al.

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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