ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

Intramolecular
Cysteine 139 and cysteine 151
Cysteine 61 and cysteine 62
Cysteine 125 and cysteine 151
Cysteine 125 and cysteine 139
Cysteine 125 and cysteine 175
A redox-regulated disulphide may form within N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) between cysteines 139 and 151.

Details

Redox score ?
71
PDB code
3nh4
Structure name
crystal structure of murine aminoacylase 3
Structure deposition date
2010-06-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q91XE4
Residue number A
139
Residue number B
151
Peptide name
N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

Ligandability

Cysteine 139 of N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

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 151 of N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

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 N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) between cysteines 61 and 62. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
3nh8
Structure name
crystal structure of murine aminoacylase 3 in complex with n-acetyl-s- 1,2-dichlorovinyl-l-cysteine
Structure deposition date
2010-06-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
10
Peptide accession
Q91XE4
Residue number A
61
Residue number B
62
Peptide name
N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

Ligandability

Cysteine 61 of N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

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 62 of N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

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 N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) between cysteines 125 and 151. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3nfz
Structure name
crystal structure of murine aminoacylase 3 in complex with n-acetyl-l- tyrosine
Structure deposition date
2010-06-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
8
% buried
94
Peptide accession
Q91XE4
Residue number A
125
Residue number B
151
Peptide name
N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

Ligandability

Cysteine 125 of N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

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 151 of N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

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 N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) between cysteines 125 and 139. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3nh8
Structure name
crystal structure of murine aminoacylase 3 in complex with n-acetyl-s- 1,2-dichlorovinyl-l-cysteine
Structure deposition date
2010-06-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
100
Peptide accession
Q91XE4
Residue number A
125
Residue number B
139
Peptide name
N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

Ligandability

Cysteine 125 of N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

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 139 of N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

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 N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) between cysteines 125 and 175. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
3nh8
Structure name
crystal structure of murine aminoacylase 3 in complex with n-acetyl-s- 1,2-dichlorovinyl-l-cysteine
Structure deposition date
2010-06-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
13
% buried
100
Peptide accession
Q91XE4
Residue number A
125
Residue number B
175
Peptide name
N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

Ligandability

Cysteine 125 of N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

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 175 of N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

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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