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a tool for identifying drug-targetable redox-active disulphides

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Adenosylhomocysteinase 3

Intramolecular
Cysteine 407 and cysteine 454
Cysteine 374 and cysteine 407 L
Cysteine 187 and cysteine 292
Cysteine 407 and cysteine 408
Cysteine 232 and cysteine 258
Cysteine 407 and cysteine 476
Cysteine 373 and cysteine 374 L
Cysteine 232 and cysteine 296
Cysteine 408 and cysteine 454
Cysteine 398 and cysteine 454
More...
Cysteine 476 and cysteine 528
Cysteine 374 and cysteine 454 L
Cysteine 292 and cysteine 296
Cysteine 454 and cysteine 476
Cysteine 253 and cysteine 296
Cysteine 473 and cysteine 476
Cysteine 398 and cysteine 408
Cysteine 232 and cysteine 292
A redox-regulated disulphide may form within Adenosylhomocysteinase 3 between cysteines 407 and 454.

Details

Redox score ?
63
PDB code
3gvp
Structure name
human sahh-like domain of human adenosylhomocysteinase 3
Structure deposition date
2009-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
91
Minimum pKa ?
9
% buried
100
Peptide accession
Q96HN2
Residue number A
407
Residue number B
454
Peptide name
Adenosylhomocysteinase 3

Ligandability

Cysteine 407 of Adenosylhomocysteinase 3

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 454 of Adenosylhomocysteinase 3

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 3 between cysteines 374 and 407. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
3gvp
Structure name
human sahh-like domain of human adenosylhomocysteinase 3
Structure deposition date
2009-03-31
Thiol separation (Å)
5
Half-sphere exposure sum ?
92
Minimum pKa ?
9
% buried
95
Peptide accession
Q96HN2
Residue number A
374
Residue number B
407
Peptide name
Adenosylhomocysteinase 3

Ligandability

Cysteine 374 of Adenosylhomocysteinase 3

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 407 of Adenosylhomocysteinase 3

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 3 between cysteines 187 and 292. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
3gvp
Structure name
human sahh-like domain of human adenosylhomocysteinase 3
Structure deposition date
2009-03-31
Thiol separation (Å)
6
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
70
Peptide accession
Q96HN2
Residue number A
187
Residue number B
292
Peptide name
Adenosylhomocysteinase 3

Ligandability

Cysteine 187 of Adenosylhomocysteinase 3

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 292 of Adenosylhomocysteinase 3

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 3 between cysteines 407 and 408. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
3gvp
Structure name
human sahh-like domain of human adenosylhomocysteinase 3
Structure deposition date
2009-03-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
93
Minimum pKa ?
9
% buried
100
Peptide accession
Q96HN2
Residue number A
407
Residue number B
408
Peptide name
Adenosylhomocysteinase 3

Ligandability

Cysteine 407 of Adenosylhomocysteinase 3

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 408 of Adenosylhomocysteinase 3

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 3 between cysteines 232 and 258. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3gvp
Structure name
human sahh-like domain of human adenosylhomocysteinase 3
Structure deposition date
2009-03-31
Thiol separation (Å)
5
Half-sphere exposure sum ?
89
Minimum pKa ?
15
% buried
99
Peptide accession
Q96HN2
Residue number A
232
Residue number B
258
Peptide name
Adenosylhomocysteinase 3

Ligandability

Cysteine 232 of Adenosylhomocysteinase 3

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 258 of Adenosylhomocysteinase 3

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 3 between cysteines 407 and 476. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
3gvp
Structure name
human sahh-like domain of human adenosylhomocysteinase 3
Structure deposition date
2009-03-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
96
Minimum pKa ?
9
% buried
100
Peptide accession
Q96HN2
Residue number A
407
Residue number B
476
Peptide name
Adenosylhomocysteinase 3

Ligandability

Cysteine 407 of Adenosylhomocysteinase 3

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 476 of Adenosylhomocysteinase 3

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 3 between cysteines 373 and 374. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3gvp
Structure name
human sahh-like domain of human adenosylhomocysteinase 3
Structure deposition date
2009-03-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
13
% buried
100
Peptide accession
Q96HN2
Residue number A
373
Residue number B
374
Peptide name
Adenosylhomocysteinase 3

Ligandability

Cysteine 373 of Adenosylhomocysteinase 3

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 374 of Adenosylhomocysteinase 3

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.

A redox-regulated disulphide may form within Adenosylhomocysteinase 3 between cysteines 232 and 296. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
3gvp
Structure name
human sahh-like domain of human adenosylhomocysteinase 3
Structure deposition date
2009-03-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
87
Minimum pKa ?
13
% buried
100
Peptide accession
Q96HN2
Residue number A
232
Residue number B
296
Peptide name
Adenosylhomocysteinase 3

Ligandability

Cysteine 232 of Adenosylhomocysteinase 3

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 296 of Adenosylhomocysteinase 3

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 3 between cysteines 408 and 454. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3gvp
Structure name
human sahh-like domain of human adenosylhomocysteinase 3
Structure deposition date
2009-03-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
91
Minimum pKa ?
13
% buried
100
Peptide accession
Q96HN2
Residue number A
408
Residue number B
454
Peptide name
Adenosylhomocysteinase 3

Ligandability

Cysteine 408 of Adenosylhomocysteinase 3

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 454 of Adenosylhomocysteinase 3

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 3 between cysteines 398 and 454. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
3gvp
Structure name
human sahh-like domain of human adenosylhomocysteinase 3
Structure deposition date
2009-03-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
95
Minimum pKa ?
12
% buried
100
Peptide accession
Q96HN2
Residue number A
398
Residue number B
454
Peptide name
Adenosylhomocysteinase 3

Ligandability

Cysteine 398 of Adenosylhomocysteinase 3

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 454 of Adenosylhomocysteinase 3

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 3 between cysteines 476 and 528. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3gvp
Structure name
human sahh-like domain of human adenosylhomocysteinase 3
Structure deposition date
2009-03-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
11
% buried
78
Peptide accession
Q96HN2
Residue number A
476
Residue number B
528
Peptide name
Adenosylhomocysteinase 3

Ligandability

Cysteine 476 of Adenosylhomocysteinase 3

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 528 of Adenosylhomocysteinase 3

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 3 between cysteines 374 and 454. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
3gvp
Structure name
human sahh-like domain of human adenosylhomocysteinase 3
Structure deposition date
2009-03-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
88
Minimum pKa ?
14
% buried
100
Peptide accession
Q96HN2
Residue number A
374
Residue number B
454
Peptide name
Adenosylhomocysteinase 3

Ligandability

Cysteine 374 of Adenosylhomocysteinase 3

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 454 of Adenosylhomocysteinase 3

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 3 between cysteines 292 and 296. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
3gvp
Structure name
human sahh-like domain of human adenosylhomocysteinase 3
Structure deposition date
2009-03-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
88
Peptide accession
Q96HN2
Residue number A
292
Residue number B
296
Peptide name
Adenosylhomocysteinase 3

Ligandability

Cysteine 292 of Adenosylhomocysteinase 3

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 296 of Adenosylhomocysteinase 3

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 3 between cysteines 454 and 476. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
3gvp
Structure name
human sahh-like domain of human adenosylhomocysteinase 3
Structure deposition date
2009-03-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
94
Minimum pKa ?
13
% buried
100
Peptide accession
Q96HN2
Residue number A
454
Residue number B
476
Peptide name
Adenosylhomocysteinase 3

Ligandability

Cysteine 454 of Adenosylhomocysteinase 3

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 476 of Adenosylhomocysteinase 3

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 3 between cysteines 253 and 296. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
3gvp
Structure name
human sahh-like domain of human adenosylhomocysteinase 3
Structure deposition date
2009-03-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
100
Peptide accession
Q96HN2
Residue number A
253
Residue number B
296
Peptide name
Adenosylhomocysteinase 3

Ligandability

Cysteine 253 of Adenosylhomocysteinase 3

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 296 of Adenosylhomocysteinase 3

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 3 between cysteines 473 and 476. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
3gvp
Structure name
human sahh-like domain of human adenosylhomocysteinase 3
Structure deposition date
2009-03-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
100
Peptide accession
Q96HN2
Residue number A
473
Residue number B
476
Peptide name
Adenosylhomocysteinase 3

Ligandability

Cysteine 473 of Adenosylhomocysteinase 3

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 476 of Adenosylhomocysteinase 3

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 3 between cysteines 398 and 408. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
3gvp
Structure name
human sahh-like domain of human adenosylhomocysteinase 3
Structure deposition date
2009-03-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
96
Minimum pKa ?
12
% buried
100
Peptide accession
Q96HN2
Residue number A
398
Residue number B
408
Peptide name
Adenosylhomocysteinase 3

Ligandability

Cysteine 398 of Adenosylhomocysteinase 3

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 408 of Adenosylhomocysteinase 3

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 3 between cysteines 232 and 292. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
3gvp
Structure name
human sahh-like domain of human adenosylhomocysteinase 3
Structure deposition date
2009-03-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
14
% buried
88
Peptide accession
Q96HN2
Residue number A
232
Residue number B
292
Peptide name
Adenosylhomocysteinase 3

Ligandability

Cysteine 232 of Adenosylhomocysteinase 3

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 292 of Adenosylhomocysteinase 3

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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