ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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FAD-linked sulfhydryl oxidase ALR

Intermolecular
Cysteine 197 and cysteine 88
Intramolecular
Cysteine 171 and cysteine 188
Cysteine 142 and cysteine 145
A redox-regulated disulphide may form between two units of FAD-linked sulfhydryl oxidase ALR at cysteines 197 and 88 (124 and 15 respectively in this structure).

Details

Redox score ?
89
PDB code
3r7c
Structure name
the structure of a hexahestidine-tagged form of augmenter of liver regeneration reveals a novel cd(2)cl(4)o(6) cluster that aids in crystal packing
Structure deposition date
2011-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
FAD-linked sulfhydryl oxidase ALR
Peptide B name
FAD-linked sulfhydryl oxidase ALR
Peptide A accession
Q63042
Peptide B accession
Q63042
Peptide A residue number
197
Peptide B residue number
88

Ligandability

Cysteine 197 of FAD-linked sulfhydryl oxidase ALR

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 88 of FAD-linked sulfhydryl oxidase ALR

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 FAD-linked sulfhydryl oxidase ALR between cysteines 171 and 188.

Details

Redox score ?
86
PDB code
3u2m
Structure name
crystal structure of human alr mutant c142/145s
Structure deposition date
2011-10-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P55789
Residue number A
171
Residue number B
188
Peptide name
FAD-linked sulfhydryl oxidase ALR

Ligandability

Cysteine 171 of FAD-linked sulfhydryl oxidase ALR

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 188 of FAD-linked sulfhydryl oxidase ALR

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 FAD-linked sulfhydryl oxidase ALR between cysteines 142 and 145.

Details

Redox score ?
83
PDB code
3mbg
Structure name
crystal structure of human augmenter of liver regeneration (alr)
Structure deposition date
2010-03-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P55789
Residue number A
142
Residue number B
145
Peptide name
FAD-linked sulfhydryl oxidase ALR

Ligandability

Cysteine 142 of FAD-linked sulfhydryl oxidase ALR

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 145 of FAD-linked sulfhydryl oxidase ALR

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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