ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Xaa-Pro dipeptidase

Intermolecular
Cysteine 158 and cysteine 58 L
Intramolecular
Cysteine 243 and cysteine 245
Cysteine 478 and cysteine 482 L
Cysteine 230 and cysteine 243
Cysteine 290 and cysteine 478
Cysteine 31 and cysteine 183
Cysteine 243 and cysteine 273
Cysteine 245 and cysteine 273
A redox-regulated disulphide is known to form between two units of Xaa-Pro dipeptidase at cysteines 158 and 58 (159 and 59 respectively in this structure).

Details

Redox score ?
84
PDB code
2iw2
Structure name
crystal structure of human prolidase
Structure deposition date
2006-06-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
5
% buried
74
Peptide A name
Xaa-Pro dipeptidase
Peptide B name
Xaa-Pro dipeptidase
Peptide A accession
P12955
Peptide B accession
P12955
Peptide A residue number
158
Peptide B residue number
58

Ligandability

Cysteine 158 of Xaa-Pro dipeptidase

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 58 of Xaa-Pro dipeptidase

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 within Xaa-Pro dipeptidase between cysteines 243 and 245. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
5mbz
Structure name
crystal structure of ser202phe mutant of human prolidase with mn ions and glypro ligand
Structure deposition date
2016-11-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
11
% buried
100
Peptide accession
P12955
Residue number A
243
Residue number B
245
Peptide name
Xaa-Pro dipeptidase

Ligandability

Cysteine 243 of Xaa-Pro dipeptidase

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 245 of Xaa-Pro dipeptidase

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 Xaa-Pro dipeptidase between cysteines 478 and 482. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
6qsb
Structure name
crystal structure of arg470his mutant of human prolidase with mn ions
Structure deposition date
2019-02-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
32
Peptide accession
P12955
Residue number A
478
Residue number B
482
Peptide name
Xaa-Pro dipeptidase

Ligandability

Cysteine 478 of Xaa-Pro dipeptidase

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 482 of Xaa-Pro dipeptidase

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.

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 Xaa-Pro dipeptidase between cysteines 230 and 243. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5mc4
Structure name
crystal structure of gly448arg mutant of human prolidase with mn ions and glypro ligand
Structure deposition date
2016-11-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
100
Peptide accession
P12955
Residue number A
230
Residue number B
243
Peptide name
Xaa-Pro dipeptidase

Ligandability

Cysteine 230 of Xaa-Pro dipeptidase

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 243 of Xaa-Pro dipeptidase

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 Xaa-Pro dipeptidase between cysteines 290 and 478 (290 and 477 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
5mc5
Structure name
crystal structure of delglu452 mutant of human prolidase with mn ions and glypro ligand
Structure deposition date
2016-11-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
71
Peptide accession
P12955
Residue number A
290
Residue number B
478
Peptide name
Xaa-Pro dipeptidase

Ligandability

Cysteine 290 of Xaa-Pro dipeptidase

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 478 of Xaa-Pro dipeptidase

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 Xaa-Pro dipeptidase between cysteines 31 and 183 (32 and 184 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
2iw2
Structure name
crystal structure of human prolidase
Structure deposition date
2006-06-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
75
Peptide accession
P12955
Residue number A
31
Residue number B
183
Peptide name
Xaa-Pro dipeptidase

Ligandability

Cysteine 31 of Xaa-Pro dipeptidase

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 183 of Xaa-Pro dipeptidase

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 Xaa-Pro dipeptidase between cysteines 243 and 273 (245 and 273 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
5mc2
Structure name
crystal structure of gly278asp mutant of human prolidase with mn ions and glypro ligand
Structure deposition date
2016-11-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
88
Minimum pKa ?
12
% buried
97
Peptide accession
P12955
Residue number A
243
Residue number B
273
Peptide name
Xaa-Pro dipeptidase

Ligandability

Cysteine 243 of Xaa-Pro dipeptidase

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 273 of Xaa-Pro dipeptidase

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 Xaa-Pro dipeptidase between cysteines 245 and 273 (246 and 274 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
2iw2
Structure name
crystal structure of human prolidase
Structure deposition date
2006-06-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
98
Minimum pKa ?
13
% buried
100
Peptide accession
P12955
Residue number A
245
Residue number B
273
Peptide name
Xaa-Pro dipeptidase

Ligandability

Cysteine 245 of Xaa-Pro dipeptidase

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 273 of Xaa-Pro dipeptidase

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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