ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Delta-aminolevulinic acid dehydratase

Intramolecular
Cysteine 124 and cysteine 132
Cysteine 119 and cysteine 162
Cysteine 122 and cysteine 124
Cysteine 122 and cysteine 132
Cysteine 75 and cysteine 162
Cysteine 75 and cysteine 119
A redox-regulated disulphide may form within Delta-aminolevulinic acid dehydratase between cysteines 124 and 132.

Details

Redox score ?
72
PDB code
5hms
Structure name
x-ray structure of human recombinant 5-aminolaevulinic acid dehydratase (hralad)
Structure deposition date
2016-01-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
83
Minimum pKa ?
8
% buried
nan
Peptide accession
P13716
Residue number A
124
Residue number B
132
Peptide name
Delta-aminolevulinic acid dehydratase

Ligandability

Cysteine 124 of Delta-aminolevulinic acid dehydratase

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 132 of Delta-aminolevulinic acid dehydratase

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 Delta-aminolevulinic acid dehydratase between cysteines 119 and 162.

Details

Redox score ?
72
PDB code
1e51
Structure name
crystal structure of native human erythrocyte 5-aminolaevulinic acid dehydratase
Structure deposition date
2000-07-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
89
Minimum pKa ?
9
% buried
100
Peptide accession
P13716
Residue number A
119
Residue number B
162
Peptide name
Delta-aminolevulinic acid dehydratase

Ligandability

Cysteine 119 of Delta-aminolevulinic acid dehydratase

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 162 of Delta-aminolevulinic acid dehydratase

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 Delta-aminolevulinic acid dehydratase between cysteines 122 and 124.

Details

Redox score ?
70
PDB code
5hms
Structure name
x-ray structure of human recombinant 5-aminolaevulinic acid dehydratase (hralad)
Structure deposition date
2016-01-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
85
Minimum pKa ?
8
% buried
100
Peptide accession
P13716
Residue number A
122
Residue number B
124
Peptide name
Delta-aminolevulinic acid dehydratase

Ligandability

Cysteine 122 of Delta-aminolevulinic acid dehydratase

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 124 of Delta-aminolevulinic acid dehydratase

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 Delta-aminolevulinic acid dehydratase between cysteines 122 and 132. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
5hms
Structure name
x-ray structure of human recombinant 5-aminolaevulinic acid dehydratase (hralad)
Structure deposition date
2016-01-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
86
Minimum pKa ?
20
% buried
nan
Peptide accession
P13716
Residue number A
122
Residue number B
132
Peptide name
Delta-aminolevulinic acid dehydratase

Ligandability

Cysteine 122 of Delta-aminolevulinic acid dehydratase

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 132 of Delta-aminolevulinic acid dehydratase

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 Delta-aminolevulinic acid dehydratase between cysteines 75 and 162. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5hnr
Structure name
the x-ray structure of octameric human native 5-aminolaevulinic acid dehydratase
Structure deposition date
2016-01-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
9
% buried
100
Peptide accession
P13716
Residue number A
75
Residue number B
162
Peptide name
Delta-aminolevulinic acid dehydratase

Ligandability

Cysteine 75 of Delta-aminolevulinic acid dehydratase

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 162 of Delta-aminolevulinic acid dehydratase

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 Delta-aminolevulinic acid dehydratase between cysteines 75 and 119. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
23
PDB code
5hms
Structure name
x-ray structure of human recombinant 5-aminolaevulinic acid dehydratase (hralad)
Structure deposition date
2016-01-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
100
Peptide accession
P13716
Residue number A
75
Residue number B
119
Peptide name
Delta-aminolevulinic acid dehydratase

Ligandability

Cysteine 75 of Delta-aminolevulinic acid dehydratase

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 119 of Delta-aminolevulinic acid dehydratase

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: