ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Kynurenine 3-monooxygenase

Intramolecular
Cysteine 139 and cysteine 299
Cysteine 139 and cysteine 140
Cysteine 139 and cysteine 160
Cysteine 166 and cysteine 324
Cysteine 160 and cysteine 299
Cysteine 25 and cysteine 324
Cysteine 166 and cysteine 299
A redox-regulated disulphide may form within Kynurenine 3-monooxygenase between cysteines 139 and 299. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
5x68
Structure name
crystal structure of human kmo
Structure deposition date
2017-02-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
12
% buried
82
Peptide accession
O15229
Residue number A
139
Residue number B
299
Peptide name
Kynurenine 3-monooxygenase

Ligandability

Cysteine 139 of Kynurenine 3-monooxygenase

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 299 of Kynurenine 3-monooxygenase

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 Kynurenine 3-monooxygenase between cysteines 139 and 140. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
6lkd
Structure name
in meso full-length rat kmo in complex with a pyrazoyl benzoic acid inhibitor
Structure deposition date
2019-12-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
30
Peptide accession
O88867
Residue number A
139
Residue number B
140
Peptide name
Kynurenine 3-monooxygenase

Ligandability

Cysteine 139 of Kynurenine 3-monooxygenase

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 140 of Kynurenine 3-monooxygenase

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 Kynurenine 3-monooxygenase between cysteines 139 and 160. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
5x68
Structure name
crystal structure of human kmo
Structure deposition date
2017-02-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
11
% buried
73
Peptide accession
O15229
Residue number A
139
Residue number B
160
Peptide name
Kynurenine 3-monooxygenase

Ligandability

Cysteine 139 of Kynurenine 3-monooxygenase

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 160 of Kynurenine 3-monooxygenase

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 Kynurenine 3-monooxygenase between cysteines 166 and 324. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
5x68
Structure name
crystal structure of human kmo
Structure deposition date
2017-02-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
86
Minimum pKa ?
13
% buried
100
Peptide accession
O15229
Residue number A
166
Residue number B
324
Peptide name
Kynurenine 3-monooxygenase

Ligandability

Cysteine 166 of Kynurenine 3-monooxygenase

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 324 of Kynurenine 3-monooxygenase

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 Kynurenine 3-monooxygenase between cysteines 160 and 299. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
5x68
Structure name
crystal structure of human kmo
Structure deposition date
2017-02-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
84
Peptide accession
O15229
Residue number A
160
Residue number B
299
Peptide name
Kynurenine 3-monooxygenase

Ligandability

Cysteine 160 of Kynurenine 3-monooxygenase

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 299 of Kynurenine 3-monooxygenase

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 Kynurenine 3-monooxygenase between cysteines 25 and 324. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
5x68
Structure name
crystal structure of human kmo
Structure deposition date
2017-02-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
95
Peptide accession
O15229
Residue number A
25
Residue number B
324
Peptide name
Kynurenine 3-monooxygenase

Ligandability

Cysteine 25 of Kynurenine 3-monooxygenase

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 324 of Kynurenine 3-monooxygenase

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 Kynurenine 3-monooxygenase between cysteines 166 and 299. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
22
PDB code
5x68
Structure name
crystal structure of human kmo
Structure deposition date
2017-02-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
13
% buried
95
Peptide accession
O15229
Residue number A
166
Residue number B
299
Peptide name
Kynurenine 3-monooxygenase

Ligandability

Cysteine 166 of Kynurenine 3-monooxygenase

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 299 of Kynurenine 3-monooxygenase

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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