ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

D-amino-acid oxidase

Intramolecular
Cysteine 263 and cysteine 264
Cysteine 181 and cysteine 322
Cysteine 18 and cysteine 322
A redox-regulated disulphide may form within D-amino-acid oxidase between cysteines 263 and 264. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
3w4k
Structure name
crystal structure of human daao in complex with coumpound 13
Structure deposition date
2013-01-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
70
Peptide accession
P14920
Residue number A
263
Residue number B
264
Peptide name
D-amino-acid oxidase

Ligandability

Cysteine 263 of D-amino-acid oxidase

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 264 of D-amino-acid oxidase

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 D-amino-acid oxidase between cysteines 181 and 322. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
22
PDB code
6kbp
Structure name
crystal structure of human d-amino acid oxidase mutant (p219l) complexed with benzoate
Structure deposition date
2019-06-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
88
Minimum pKa ?
13
% buried
100
Peptide accession
P14920
Residue number A
181
Residue number B
322
Peptide name
D-amino-acid oxidase

Ligandability

Cysteine 181 of D-amino-acid oxidase

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 322 of D-amino-acid oxidase

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 D-amino-acid oxidase between cysteines 18 and 322. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
21
PDB code
5wx2
Structure name
crystal structure of porcine kidney d-amino acid oxidase mutant (i230a/r283g)
Structure deposition date
2017-01-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
96
Peptide accession
P00371
Residue number A
18
Residue number B
322
Peptide name
D-amino-acid oxidase

Ligandability

Cysteine 18 of D-amino-acid oxidase

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 322 of D-amino-acid oxidase

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.

If this tool was useful for finding a disulphide, please cite: