ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Adenosylhomocysteinase

Intramolecular
Cysteine 195 and cysteine 228 L
Cysteine 53 and cysteine 79
Cysteine 228 and cysteine 297
Cysteine 297 and cysteine 349
Cysteine 53 and cysteine 113
A redox-regulated disulphide may form within Adenosylhomocysteinase between cysteines 195 and 228 (194 and 227 respectively in this structure).

Details

Redox score ?
63
PDB code
1d4f
Structure name
crystal structure of recombinant rat-liver d244e mutant s- adenosylhomocysteine hydrolase
Structure deposition date
2000-06-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
97
Minimum pKa ?
9
% buried
100
Peptide accession
P10760
Residue number A
195
Residue number B
228
Peptide name
Adenosylhomocysteinase

Ligandability

Cysteine 195 of Adenosylhomocysteinase

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 228 of Adenosylhomocysteinase

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 Adenosylhomocysteinase between cysteines 53 and 79 (52 and 78 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
1b3r
Structure name
rat liver s-adenosylhomocystein hydrolase
Structure deposition date
1998-12-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
86
Minimum pKa ?
9
% buried
100
Peptide accession
P10760
Residue number A
53
Residue number B
79
Peptide name
Adenosylhomocysteinase

Ligandability

Cysteine 53 of Adenosylhomocysteinase

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 79 of Adenosylhomocysteinase

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 Adenosylhomocysteinase between cysteines 228 and 297. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
5axc
Structure name
crystal structure of mouse sahh complexed with 3'-keto aristeromycin
Structure deposition date
2015-07-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
100
Minimum pKa ?
10
% buried
100
Peptide accession
P50247
Residue number A
228
Residue number B
297
Peptide name
Adenosylhomocysteinase

Ligandability

Cysteine 228 of Adenosylhomocysteinase

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 297 of Adenosylhomocysteinase

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 Adenosylhomocysteinase between cysteines 297 and 349. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
5axb
Structure name
crystal structure of mouse sahh complexed with noraristeromycin
Structure deposition date
2015-07-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
90
Minimum pKa ?
11
% buried
100
Peptide accession
P50247
Residue number A
297
Residue number B
349
Peptide name
Adenosylhomocysteinase

Ligandability

Cysteine 297 of Adenosylhomocysteinase

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 349 of Adenosylhomocysteinase

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 Adenosylhomocysteinase between cysteines 53 and 113 (52 and 112 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
1d4f
Structure name
crystal structure of recombinant rat-liver d244e mutant s- adenosylhomocysteine hydrolase
Structure deposition date
2000-06-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
13
% buried
86
Peptide accession
P10760
Residue number A
53
Residue number B
113
Peptide name
Adenosylhomocysteinase

Ligandability

Cysteine 53 of Adenosylhomocysteinase

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 113 of Adenosylhomocysteinase

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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