ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Beta-hexosaminidase subunit alpha

Intramolecular
Cysteine 58 and cysteine 104 L
Cysteine 277 and cysteine 328
Cysteine 505 and cysteine 522
A redox-regulated disulphide may form within Beta-hexosaminidase subunit alpha between cysteines 58 and 104.

Details

Redox score ?
87
PDB code
2gjx
Structure name
crystallographic structure of human beta-hexosaminidase a
Structure deposition date
2006-03-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P06865
Residue number A
58
Residue number B
104
Peptide name
Beta-hexosaminidase subunit alpha

Ligandability

Cysteine 58 of Beta-hexosaminidase subunit alpha

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 104 of Beta-hexosaminidase subunit alpha

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 Beta-hexosaminidase subunit alpha between cysteines 277 and 328.

Details

Redox score ?
84
PDB code
2gjx
Structure name
crystallographic structure of human beta-hexosaminidase a
Structure deposition date
2006-03-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P06865
Residue number A
277
Residue number B
328
Peptide name
Beta-hexosaminidase subunit alpha

Ligandability

Cysteine 277 of Beta-hexosaminidase subunit alpha

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 328 of Beta-hexosaminidase subunit alpha

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 Beta-hexosaminidase subunit alpha between cysteines 505 and 522.

Details

Redox score ?
83
PDB code
2gk1
Structure name
x-ray crystal structure of ngt-bound hexa
Structure deposition date
2006-03-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P06865
Residue number A
505
Residue number B
522
Peptide name
Beta-hexosaminidase subunit alpha

Ligandability

Cysteine 505 of Beta-hexosaminidase subunit alpha

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 522 of Beta-hexosaminidase subunit alpha

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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