ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Myeloperoxidase

Intermolecular
Cysteine 319 and cysteine 319
Intramolecular
Cysteine 158 and cysteine 319
Cysteine 281 and cysteine 291
Cysteine 285 and cysteine 309
Cysteine 167 and cysteine 180
Cysteine 704 and cysteine 730
Cysteine 606 and cysteine 663
Cysteine 387 and cysteine 398
Cysteine 291 and cysteine 309
Cysteine 281 and cysteine 285
More...
Cysteine 281 and cysteine 309
Cysteine 285 and cysteine 291
A redox-regulated disulphide may form between two units of Myeloperoxidase at cysteines 319 and 319 (153 and 153 respectively in this structure).

Details

Redox score ?
85
PDB code
1cxp
Structure name
cryogenic crystal structure of human myeloperoxidase isoform c
Structure deposition date
1999-08-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide A name
Myeloperoxidase
Peptide B name
Myeloperoxidase
Peptide A accession
P05164
Peptide B accession
P05164
Peptide A residue number
319
Peptide B residue number
319

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 within Myeloperoxidase between cysteines 158 and 319.

Details

Redox score ?
84
PDB code
5mfa
Structure name
crystal structure of human promyeloperoxidase (prompo)
Structure deposition date
2016-11-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05164
Residue number A
158
Residue number B
319
Peptide name
Myeloperoxidase

Ligandability

Cysteine 158 of Myeloperoxidase

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 319 of Myeloperoxidase

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 Myeloperoxidase between cysteines 281 and 291 (115 and 125 respectively in this structure).

Details

Redox score ?
84
PDB code
6wy0
Structure name
crystal structure of myeloperoxidase subform c (mpo) complex with compound-40 a
Structure deposition date
2020-05-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
22
Peptide accession
P05164
Residue number A
281
Residue number B
291
Peptide name
Myeloperoxidase

Ligandability

Cysteine 281 of Myeloperoxidase

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 291 of Myeloperoxidase

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 Myeloperoxidase between cysteines 285 and 309 (119 and 143 respectively in this structure).

Details

Redox score ?
81
PDB code
6wy5
Structure name
crystal structure of myeloperoxidase subform c (mpo) complex with compound-37 a
Structure deposition date
2020-05-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
28
Peptide accession
P05164
Residue number A
285
Residue number B
309
Peptide name
Myeloperoxidase

Ligandability

Cysteine 285 of Myeloperoxidase

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 309 of Myeloperoxidase

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 Myeloperoxidase between cysteines 167 and 180 (1 and 14 respectively in this structure).

Details

Redox score ?
79
PDB code
6wyd
Structure name
crystal structure of myeloperoxidase subform c (mpo) complex with compound-12 (aka; 7-benzyl-1h-[1,2,3]triazolo[4,5-b]pyrid
Structure deposition date
2020-05-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
nan
Peptide accession
P05164
Residue number A
167
Residue number B
180
Peptide name
Myeloperoxidase

Ligandability

Cysteine 167 of Myeloperoxidase

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 180 of Myeloperoxidase

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 Myeloperoxidase between cysteines 704 and 730 (538 and 564 respectively in this structure).

Details

Redox score ?
78
PDB code
6wy0
Structure name
crystal structure of myeloperoxidase subform c (mpo) complex with compound-40 a
Structure deposition date
2020-05-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
46
Peptide accession
P05164
Residue number A
704
Residue number B
730
Peptide name
Myeloperoxidase

Ligandability

Cysteine 704 of Myeloperoxidase

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 730 of Myeloperoxidase

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 Myeloperoxidase between cysteines 606 and 663 (440 and 497 respectively in this structure).

Details

Redox score ?
78
PDB code
6wy5
Structure name
crystal structure of myeloperoxidase subform c (mpo) complex with compound-37 a
Structure deposition date
2020-05-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
7
% buried
98
Peptide accession
P05164
Residue number A
606
Residue number B
663
Peptide name
Myeloperoxidase

Ligandability

Cysteine 606 of Myeloperoxidase

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 663 of Myeloperoxidase

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 Myeloperoxidase between cysteines 387 and 398 (221 and 232 respectively in this structure).

Details

Redox score ?
76
PDB code
6wy5
Structure name
crystal structure of myeloperoxidase subform c (mpo) complex with compound-37 a
Structure deposition date
2020-05-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
79
Minimum pKa ?
8
% buried
88
Peptide accession
P05164
Residue number A
387
Residue number B
398
Peptide name
Myeloperoxidase

Ligandability

Cysteine 387 of Myeloperoxidase

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 398 of Myeloperoxidase

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 Myeloperoxidase between cysteines 291 and 309 (125 and 143 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
7ni3
Structure name
crystal structure of native human myeloperoxidase in complex with cpd 3
Structure deposition date
2021-02-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05164
Residue number A
291
Residue number B
309
Peptide name
Myeloperoxidase

Ligandability

Cysteine 291 of Myeloperoxidase

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 309 of Myeloperoxidase

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 Myeloperoxidase between cysteines 281 and 285 (115 and 119 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
1myp
Structure name
x-ray crystal structure of canine myeloperoxidase at 3 angstroms resolution
Structure deposition date
1992-04-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05164
Residue number A
281
Residue number B
285
Peptide name
Myeloperoxidase

Ligandability

Cysteine 281 of Myeloperoxidase

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 285 of Myeloperoxidase

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 Myeloperoxidase between cysteines 281 and 309. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6bmt
Structure name
crystal structure of a recombinant form of human myeloperoxidase bound to an inhibitor from staphylococcus delphini
Structure deposition date
2017-11-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05164
Residue number A
281
Residue number B
309
Peptide name
Myeloperoxidase

Ligandability

Cysteine 281 of Myeloperoxidase

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 309 of Myeloperoxidase

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 Myeloperoxidase between cysteines 285 and 291 (119 and 125 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
7lal
Structure name
crystal structure of myeloperoxidase subform c (mpo) complex with compound-18 aka 7-(3-(2,3-dihydro-1h-inden-1-ylamino)-1- phenylpropyl)-1h-[1,2,3]triazolo[4,5-b]pyridin-5-amine
Structure deposition date
2021-01-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
nan
Peptide accession
P05164
Residue number A
285
Residue number B
291
Peptide name
Myeloperoxidase

Ligandability

Cysteine 285 of Myeloperoxidase

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 291 of Myeloperoxidase

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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