ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Lactoperoxidase

Intramolecular
Cysteine 123 and cysteine 284
Cysteine 671 and cysteine 696
Cysteine 132 and cysteine 145
Cysteine 250 and cysteine 274
Cysteine 246 and cysteine 256
Cysteine 573 and cysteine 630
Cysteine 354 and cysteine 365
Cysteine 246 and cysteine 274
Cysteine 246 and cysteine 250
Cysteine 250 and cysteine 256
Cysteine 256 and cysteine 274
A redox-regulated disulphide may form within Lactoperoxidase between cysteines 123 and 284 (6 and 167 respectively in this structure).

Details

Redox score ?
86
PDB code
3erh
Structure name
first structural evidence of substrate specificity in mammalian peroxidases: crystal structures of substrate complexes with lactoperoxidases from two different species
Structure deposition date
2008-10-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
A5JUY8
Residue number A
123
Residue number B
284
Peptide name
Lactoperoxidase

Ligandability

Cysteine 123 of Lactoperoxidase

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 284 of Lactoperoxidase

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 Lactoperoxidase between cysteines 671 and 696 (554 and 579 respectively in this structure).

Details

Redox score ?
86
PDB code
2efb
Structure name
crystal structure of the complex of goat lactoperoxidase with phosphate at 2
Structure deposition date
2007-02-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
A3F9D6
Residue number A
671
Residue number B
696
Peptide name
Lactoperoxidase

Ligandability

Cysteine 671 of Lactoperoxidase

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 696 of Lactoperoxidase

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 Lactoperoxidase between cysteines 132 and 145 (15 and 28 respectively in this structure).

Details

Redox score ?
85
PDB code
6m7e
Structure name
structure of bovine lactoperoxidase with multiple iodide ions in the distaline heme cavity
Structure deposition date
2020-03-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P80025
Residue number A
132
Residue number B
145
Peptide name
Lactoperoxidase

Ligandability

Cysteine 132 of Lactoperoxidase

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 145 of Lactoperoxidase

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 Lactoperoxidase between cysteines 250 and 274 (133 and 157 respectively in this structure).

Details

Redox score ?
84
PDB code
3erh
Structure name
first structural evidence of substrate specificity in mammalian peroxidases: crystal structures of substrate complexes with lactoperoxidases from two different species
Structure deposition date
2008-10-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
A5JUY8
Residue number A
250
Residue number B
274
Peptide name
Lactoperoxidase

Ligandability

Cysteine 250 of Lactoperoxidase

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 274 of Lactoperoxidase

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 Lactoperoxidase between cysteines 246 and 256 (129 and 139 respectively in this structure).

Details

Redox score ?
84
PDB code
7wcs
Structure name
structure of the lactoperoxidase with bound nitric oxide and nitrite in the substrate binding site at 1
Structure deposition date
2021-12-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
A0A452E9Y6
Residue number A
246
Residue number B
256
Peptide name
Lactoperoxidase

Ligandability

Cysteine 246 of Lactoperoxidase

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 256 of Lactoperoxidase

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 Lactoperoxidase between cysteines 573 and 630 (456 and 513 respectively in this structure).

Details

Redox score ?
81
PDB code
3i6n
Structure name
mode of binding of the tuberculosis prodrug isoniazid to peroxidases: crystal structure of bovine lactoperoxidase with isoniazid at 2
Structure deposition date
2009-07-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P80025
Residue number A
573
Residue number B
630
Peptide name
Lactoperoxidase

Ligandability

Cysteine 573 of Lactoperoxidase

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 630 of Lactoperoxidase

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 Lactoperoxidase between cysteines 354 and 365 (237 and 248 respectively in this structure).

Details

Redox score ?
81
PDB code
7dlq
Structure name
crystal structure of the complex of lactoperoxidase with hydrogen peroxide at 1
Structure deposition date
2020-11-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P80025
Residue number A
354
Residue number B
365
Peptide name
Lactoperoxidase

Ligandability

Cysteine 354 of Lactoperoxidase

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 365 of Lactoperoxidase

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 Lactoperoxidase between cysteines 246 and 274 (129 and 157 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
6lf7
Structure name
crystal structure of the complex of goat lactoperoxidase with hypothiocyanite and hydrogen peroxide at 1
Structure deposition date
2019-11-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
A0A452E9Y6
Residue number A
246
Residue number B
274
Peptide name
Lactoperoxidase

Ligandability

Cysteine 246 of Lactoperoxidase

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 274 of Lactoperoxidase

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 Lactoperoxidase between cysteines 246 and 250 (129 and 133 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
6lf7
Structure name
crystal structure of the complex of goat lactoperoxidase with hypothiocyanite and hydrogen peroxide at 1
Structure deposition date
2019-11-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
A0A452E9Y6
Residue number A
246
Residue number B
250
Peptide name
Lactoperoxidase

Ligandability

Cysteine 246 of Lactoperoxidase

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 250 of Lactoperoxidase

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 Lactoperoxidase between cysteines 250 and 256 (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 ?
55
PDB code
2gjm
Structure name
crystal structure of buffalo lactoperoxidase at 2
Structure deposition date
2006-03-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
A5JUY8
Residue number A
250
Residue number B
256
Peptide name
Lactoperoxidase

Ligandability

Cysteine 250 of Lactoperoxidase

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 256 of Lactoperoxidase

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 Lactoperoxidase between cysteines 256 and 274 (139 and 157 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
3faq
Structure name
crystal structure of lactoperoxidase complex with cyanide
Structure deposition date
2008-11-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
A5JUY8
Residue number A
256
Residue number B
274
Peptide name
Lactoperoxidase

Ligandability

Cysteine 256 of Lactoperoxidase

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 274 of Lactoperoxidase

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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