ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Fructose-bisphosphate aldolase A

Intramolecular
Cysteine 135 and cysteine 178
Cysteine 202 and cysteine 240
Cysteine 73 and cysteine 339
A redox-regulated disulphide may form within Fructose-bisphosphate aldolase A between cysteines 135 and 178.

Details

Redox score ?
72
PDB code
6xml
Structure name
human aldolase a i98c
Structure deposition date
2020-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
84
Minimum pKa ?
8
% buried
87
Peptide accession
P04075
Residue number A
135
Residue number B
178
Peptide name
Fructose-bisphosphate aldolase A

Ligandability

Cysteine 135 of Fructose-bisphosphate aldolase A

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 178 of Fructose-bisphosphate aldolase A

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 Fructose-bisphosphate aldolase A between cysteines 202 and 240 (201 and 239 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
8ew2
Structure name
cryo-em structure of aldolase embedded in crystalline ice
Structure deposition date
2022-10-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
49
Peptide accession
P00883
Residue number A
202
Residue number B
240
Peptide name
Fructose-bisphosphate aldolase A

Ligandability

Cysteine 202 of Fructose-bisphosphate aldolase A

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 240 of Fructose-bisphosphate aldolase A

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 Fructose-bisphosphate aldolase A between cysteines 73 and 339. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6xmo
Structure name
human aldolase a i98f
Structure deposition date
2020-06-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
11
% buried
72
Peptide accession
P04075
Residue number A
73
Residue number B
339
Peptide name
Fructose-bisphosphate aldolase A

Ligandability

Cysteine 73 of Fructose-bisphosphate aldolase A

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 339 of Fructose-bisphosphate aldolase A

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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