ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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2-Hydroxyacid oxidase 2

Intramolecular
Cysteine 74 and cysteine 298
Cysteine 74 and cysteine 102
Cysteine 331 and cysteine 337
Cysteine 102 and cysteine 298
A redox-regulated disulphide may form within 2-Hydroxyacid oxidase 2 between cysteines 74 and 298 (73 and 297 respectively in this structure).

Details

Redox score ?
65
PDB code
1tb3
Structure name
crystal structure analysis of recombinant rat kidney long- chain hydroxy acid oxidase
Structure deposition date
2004-05-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
94
Minimum pKa ?
9
% buried
100
Peptide accession
Q07523
Residue number A
74
Residue number B
298
Peptide name
2-Hydroxyacid oxidase 2

Ligandability

Cysteine 74 of 2-Hydroxyacid oxidase 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 298 of 2-Hydroxyacid oxidase 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.

A redox-regulated disulphide may form within 2-Hydroxyacid oxidase 2 between cysteines 74 and 102 (73 and 101 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
3sgz
Structure name
high resolution crystal structure of rat long chain hydroxy acid oxidase in complex with the inhibitor 4-carboxy-5-[(4-chiorophenyl) sulfanyl]-1, 2, 3-thiadiazole
Structure deposition date
2011-06-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
91
Minimum pKa ?
9
% buried
100
Peptide accession
Q07523
Residue number A
74
Residue number B
102
Peptide name
2-Hydroxyacid oxidase 2

Ligandability

Cysteine 74 of 2-Hydroxyacid oxidase 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 102 of 2-Hydroxyacid oxidase 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.

A redox-regulated disulphide may form within 2-Hydroxyacid oxidase 2 between cysteines 331 and 337 (330 and 336 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3sgz
Structure name
high resolution crystal structure of rat long chain hydroxy acid oxidase in complex with the inhibitor 4-carboxy-5-[(4-chiorophenyl) sulfanyl]-1, 2, 3-thiadiazole
Structure deposition date
2011-06-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
63
Peptide accession
Q07523
Residue number A
331
Residue number B
337
Peptide name
2-Hydroxyacid oxidase 2

Ligandability

Cysteine 331 of 2-Hydroxyacid oxidase 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 337 of 2-Hydroxyacid oxidase 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.

A redox-regulated disulphide may form within 2-Hydroxyacid oxidase 2 between cysteines 102 and 298 (101 and 297 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
1tb3
Structure name
crystal structure analysis of recombinant rat kidney long- chain hydroxy acid oxidase
Structure deposition date
2004-05-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
88
Minimum pKa ?
15
% buried
100
Peptide accession
Q07523
Residue number A
102
Residue number B
298
Peptide name
2-Hydroxyacid oxidase 2

Ligandability

Cysteine 102 of 2-Hydroxyacid oxidase 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 298 of 2-Hydroxyacid oxidase 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.

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