ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Beta-secretase 2

Intermolecular
Cysteine 393 and cysteine 393
Cysteine 393 and cysteine 344
Cysteine 344 and cysteine 344
Intramolecular
Cysteine 292 and cysteine 457
Cysteine 233 and cysteine 433
A redox-regulated disulphide may form between two units of Beta-secretase 2 at cysteines 393 and 393 (331 and 331 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2ewy
Structure name
crystal structure of human bace2 in complex with a hydroxyethylenamine transition-state inhibitor
Structure deposition date
2005-11-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide A name
Beta-secretase 2
Peptide B name
Beta-secretase 2
Peptide A accession
Q9Y5Z0
Peptide B accession
Q9Y5Z0
Peptide A residue number
393
Peptide B residue number
393

Ligandability

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 between two units of Beta-secretase 2 at cysteines 393 and 344 (331 and 282 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2ewy
Structure name
crystal structure of human bace2 in complex with a hydroxyethylenamine transition-state inhibitor
Structure deposition date
2005-11-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide A name
Beta-secretase 2
Peptide B name
Beta-secretase 2
Peptide A accession
Q9Y5Z0
Peptide B accession
Q9Y5Z0
Peptide A residue number
393
Peptide B residue number
344

Ligandability

Cysteine 393 of Beta-secretase 2

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 344 of Beta-secretase 2

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 between two units of Beta-secretase 2 at cysteines 344 and 344 (282 and 282 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
2ewy
Structure name
crystal structure of human bace2 in complex with a hydroxyethylenamine transition-state inhibitor
Structure deposition date
2005-11-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide A name
Beta-secretase 2
Peptide B name
Beta-secretase 2
Peptide A accession
Q9Y5Z0
Peptide B accession
Q9Y5Z0
Peptide A residue number
344
Peptide B residue number
344

Ligandability

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-secretase 2 between cysteines 292 and 457 (230 and 395 respectively in this structure).

Details

Redox score ?
87
PDB code
4bel
Structure name
bace2 xaperone complex
Structure deposition date
2013-03-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y5Z0
Residue number A
292
Residue number B
457
Peptide name
Beta-secretase 2

Ligandability

Cysteine 292 of Beta-secretase 2

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 457 of Beta-secretase 2

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-secretase 2 between cysteines 233 and 433 (171 and 371 respectively in this structure).

Details

Redox score ?
77
PDB code
6uj0
Structure name
unbound bace2 mutant structure
Structure deposition date
2019-10-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y5Z0
Residue number A
233
Residue number B
433
Peptide name
Beta-secretase 2

Ligandability

Cysteine 233 of Beta-secretase 2

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 433 of Beta-secretase 2

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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