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Cyclic GMP-AMP synthase

Intramolecular
Cysteine 396 and cysteine 397
Cysteine 405 and cysteine 463
Cysteine 397 and cysteine 404
Cysteine 405 and cysteine 409
Cysteine 384 and cysteine 438
Cysteine 404 and cysteine 405
Cysteine 409 and cysteine 467
Cysteine 396 and cysteine 405
Cysteine 396 and cysteine 404
Cysteine 405 and cysteine 467
More...
Cysteine 397 and cysteine 405
Cysteine 463 and cysteine 467
Cysteine 404 and cysteine 463
Cysteine 404 and cysteine 446
Cysteine 446 and cysteine 467
Cysteine 404 and cysteine 409
Cysteine 446 and cysteine 463
Cysteine 405 and cysteine 446
Cysteine 437 and cysteine 442
Cysteine 467 and cysteine 474
Cysteine 409 and cysteine 446
Cysteine 396 and cysteine 446
A redox-regulated disulphide may form within Cyclic GMP-AMP synthase between cysteines 396 and 397.

Details

Redox score ?
88
PDB code
5vdv
Structure name
human cyclic gmp-amp synthase (cgas) in complex with compound f3
Structure deposition date
2017-04-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
1
% buried
60
Peptide accession
Q8N884
Residue number A
396
Residue number B
397
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 396 of Cyclic GMP-AMP synthase

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 397 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 405 and 463.

Details

Redox score ?
85
PDB code
6mju
Structure name
human cgas catalytic domain bound with the inhibitor g108
Structure deposition date
2018-09-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
4
% buried
58
Peptide accession
Q8N884
Residue number A
405
Residue number B
463
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 405 of Cyclic GMP-AMP synthase

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 463 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 397 and 404.

Details

Redox score ?
81
PDB code
6lri
Structure name
human cgas catalytic domain bound with compound 17
Structure deposition date
2020-01-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
6
% buried
nan
Peptide accession
Q8N884
Residue number A
397
Residue number B
404
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 397 of Cyclic GMP-AMP synthase

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 404 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 405 and 409.

Details

Redox score ?
77
PDB code
5vdo
Structure name
human cyclic gmp-amp synthase (cgas) in complex with 2',2'-cgamp
Structure deposition date
2017-04-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
4
% buried
83
Peptide accession
Q8N884
Residue number A
405
Residue number B
409
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 405 of Cyclic GMP-AMP synthase

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 409 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 384 and 438 (386 and 440 respectively in this structure).

Details

Redox score ?
77
PDB code
4kb6
Structure name
structure of porcine cyclic gmp amp synthase (cgas) in complex with dna, atp and gtp
Structure deposition date
2013-04-23
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
4
% buried
78
Peptide accession
I3LM39
Residue number A
384
Residue number B
438
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 384 of Cyclic GMP-AMP synthase

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 438 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 404 and 405.

Details

Redox score ?
76
PDB code
5vdr
Structure name
human cyclic gmp-amp synthase (cgas) in complex with 3',3'-cdimp
Structure deposition date
2017-04-03
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
1
% buried
70
Peptide accession
Q8N884
Residue number A
404
Residue number B
405
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 404 of Cyclic GMP-AMP synthase

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 405 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 409 and 467.

Details

Redox score ?
67
PDB code
5vdt
Structure name
human cyclic gmp-amp synthase (cgas) in complex with 3',3'-cgamp
Structure deposition date
2017-04-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
9
% buried
94
Peptide accession
Q8N884
Residue number A
409
Residue number B
467
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 409 of Cyclic GMP-AMP synthase

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 467 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 396 and 405. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
6edb
Structure name
crystal structure of sry
Structure deposition date
2018-08-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
4
% buried
57
Peptide accession
Q8N884
Residue number A
396
Residue number B
405
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 396 of Cyclic GMP-AMP synthase

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 405 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 396 and 404. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
6ct9
Structure name
structure of the human cgas-dna complex
Structure deposition date
2018-03-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
19
% buried
nan
Peptide accession
Q8N884
Residue number A
396
Residue number B
404
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 396 of Cyclic GMP-AMP synthase

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 404 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 405 and 467. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
5vdu
Structure name
human cyclic gmp-amp synthase (cgas) in complex with compound f2
Structure deposition date
2017-04-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
77
Minimum pKa ?
4
% buried
84
Peptide accession
Q8N884
Residue number A
405
Residue number B
467
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 405 of Cyclic GMP-AMP synthase

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 467 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 397 and 405. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
4lev
Structure name
structure of human cgas
Structure deposition date
2013-06-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
4
% buried
nan
Peptide accession
Q8N884
Residue number A
397
Residue number B
405
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 397 of Cyclic GMP-AMP synthase

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 405 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 463 and 467. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
6lrk
Structure name
human cgas catalytic domain bound with compound 40
Structure deposition date
2020-01-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
9
% buried
73
Peptide accession
Q8N884
Residue number A
463
Residue number B
467
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 463 of Cyclic GMP-AMP synthase

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 467 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 404 and 463. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
6nfo
Structure name
cyclic gmp-amp synthase in complex with compound 20 inhibitor: 7- hydroxy-n-[(2s)-1-hydroxypropan-2-yl]-5-phenylpyrazolo[1,5- a]pyrimidine-3-carboxamide
Structure deposition date
2018-12-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
6
% buried
64
Peptide accession
Q8N884
Residue number A
404
Residue number B
463
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 404 of Cyclic GMP-AMP synthase

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 463 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 404 and 446. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
5vds
Structure name
human cyclic gmp-amp synthase (cgas) in complex with 3',3'-cdump
Structure deposition date
2017-04-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
6
% buried
86
Peptide accession
Q8N884
Residue number A
404
Residue number B
446
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 404 of Cyclic GMP-AMP synthase

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 446 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 446 and 467. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
6lri
Structure name
human cgas catalytic domain bound with compound 17
Structure deposition date
2020-01-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
10
% buried
98
Peptide accession
Q8N884
Residue number A
446
Residue number B
467
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 446 of Cyclic GMP-AMP synthase

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 467 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 404 and 409. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
5vdu
Structure name
human cyclic gmp-amp synthase (cgas) in complex with compound f2
Structure deposition date
2017-04-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
5
% buried
91
Peptide accession
Q8N884
Residue number A
404
Residue number B
409
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 404 of Cyclic GMP-AMP synthase

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 409 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 446 and 463. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
5vdq
Structure name
human cyclic gmp-amp synthase (cgas) in complex with 2',5'-gpap
Structure deposition date
2017-04-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
4
% buried
78
Peptide accession
Q8N884
Residue number A
446
Residue number B
463
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 446 of Cyclic GMP-AMP synthase

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 463 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 405 and 446. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4o67
Structure name
human cyclic gmp-amp synthase (cgas) in complex with gamp
Structure deposition date
2013-12-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
5
% buried
92
Peptide accession
Q8N884
Residue number A
405
Residue number B
446
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 405 of Cyclic GMP-AMP synthase

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 446 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 437 and 442 (439 and 444 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
4jlz
Structure name
structure of porcine cgas in complex with bound utp
Structure deposition date
2013-03-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
57
Peptide accession
I3LM39
Residue number A
437
Residue number B
442
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 437 of Cyclic GMP-AMP synthase

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 442 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 467 and 474. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6edb
Structure name
crystal structure of sry
Structure deposition date
2018-08-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
12
% buried
88
Peptide accession
Q8N884
Residue number A
467
Residue number B
474
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 467 of Cyclic GMP-AMP synthase

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 474 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 409 and 446. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
5vdv
Structure name
human cyclic gmp-amp synthase (cgas) in complex with compound f3
Structure deposition date
2017-04-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
94
Peptide accession
Q8N884
Residue number A
409
Residue number B
446
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 409 of Cyclic GMP-AMP synthase

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 446 of Cyclic GMP-AMP synthase

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 Cyclic GMP-AMP synthase between cysteines 396 and 446. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6ct9
Structure name
structure of the human cgas-dna complex
Structure deposition date
2018-03-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
13
% buried
81
Peptide accession
Q8N884
Residue number A
396
Residue number B
446
Peptide name
Cyclic GMP-AMP synthase

Ligandability

Cysteine 396 of Cyclic GMP-AMP synthase

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 446 of Cyclic GMP-AMP synthase

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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