ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Serine/threonine-protein kinase SMG1

Intermolecular
Cysteine 492 and cysteine 380 of Nonsense-mediated mRNA decay factor SMG9 L
Intramolecular
Cysteine 1130 and cysteine 1138
Cysteine 1842 and cysteine 1929
Cysteine 254 and cysteine 299
Cysteine 1081 and cysteine 1085
Cysteine 294 and cysteine 296
Cysteine 1130 and cysteine 1137
Cysteine 1137 and cysteine 1138
Cysteine 780 and cysteine 802
Cysteine 216 and cysteine 217
More...
Cysteine 798 and cysteine 802
Cysteine 217 and cysteine 222
Cysteine 1842 and cysteine 1846
Cysteine 296 and cysteine 299
Cysteine 1023 and cysteine 1085
Cysteine 489 and cysteine 492
Cysteine 1023 and cysteine 1356
Cysteine 761 and cysteine 798
Cysteine 780 and cysteine 798
Cysteine 1081 and cysteine 1193
Cysteine 776 and cysteine 780
Cysteine 1191 and cysteine 1193
A redox-regulated disulphide may form between cysteine 492 of Serine/threonine-protein kinase SMG1 and cysteine 380 of Nonsense-mediated mRNA decay factor SMG9.

Details

Redox score ?
70
PDB code
6l54
Structure name
structure of smg189
Structure deposition date
2019-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
7
% buried
100
Peptide A name
Serine/threonine-protein kinase SMG1
Peptide B name
Nonsense-mediated mRNA decay factor SMG9
Peptide A accession
Q96Q15
Peptide B accession
Q9H0W8
Peptide A residue number
492
Peptide B residue number
380

Ligandability

Cysteine 492 of Serine/threonine-protein kinase SMG1

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 380 of Nonsense-mediated mRNA decay factor SMG9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

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 Serine/threonine-protein kinase SMG1 between cysteines 1130 and 1138.

Details

Redox score ?
80
PDB code
7pw8
Structure name
human smg1-8-9 kinase complex bound to amppnp
Structure deposition date
2021-10-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
14
Peptide accession
Q96Q15
Residue number A
1130
Residue number B
1138
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 1130 of Serine/threonine-protein kinase SMG1

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 1138 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 1842 and 1929.

Details

Redox score ?
78
PDB code
6l53
Structure name
structure of smg1
Structure deposition date
2019-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
9
% buried
13
Peptide accession
Q96Q15
Residue number A
1842
Residue number B
1929
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 1842 of Serine/threonine-protein kinase SMG1

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 1929 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 254 and 299.

Details

Redox score ?
63
PDB code
6l53
Structure name
structure of smg1
Structure deposition date
2019-10-22
Thiol separation (Å)
6
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
6
Peptide accession
Q96Q15
Residue number A
254
Residue number B
299
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 254 of Serine/threonine-protein kinase SMG1

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 299 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 1081 and 1085. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
6l53
Structure name
structure of smg1
Structure deposition date
2019-10-22
Thiol separation (Å)
6
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
70
Peptide accession
Q96Q15
Residue number A
1081
Residue number B
1085
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 1081 of Serine/threonine-protein kinase SMG1

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 1085 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 294 and 296. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
6l53
Structure name
structure of smg1
Structure deposition date
2019-10-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
39
Minimum pKa ?
9
% buried
8
Peptide accession
Q96Q15
Residue number A
294
Residue number B
296
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 294 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 1130 and 1137. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
7pw4
Structure name
human smg1-8-9 kinase complex bound to a smg1 inhibitor
Structure deposition date
2021-10-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
24
Peptide accession
Q96Q15
Residue number A
1130
Residue number B
1137
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 1130 of Serine/threonine-protein kinase SMG1

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 1137 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 1137 and 1138. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
6l53
Structure name
structure of smg1
Structure deposition date
2019-10-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
47
Minimum pKa ?
10
% buried
27
Peptide accession
Q96Q15
Residue number A
1137
Residue number B
1138
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 1137 of Serine/threonine-protein kinase SMG1

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 1138 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 780 and 802. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
7pw7
Structure name
human smg1-9 kinase complex bound to a smg1 inhibitor
Structure deposition date
2021-10-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
82
Minimum pKa ?
11
% buried
84
Peptide accession
Q96Q15
Residue number A
780
Residue number B
802
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 780 of Serine/threonine-protein kinase SMG1

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 802 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 216 and 217. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
6l54
Structure name
structure of smg189
Structure deposition date
2019-10-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
24
Peptide accession
Q96Q15
Residue number A
216
Residue number B
217
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 216 of Serine/threonine-protein kinase SMG1

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 217 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 798 and 802. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
6syt
Structure name
structure of the smg1-smg8-smg9 complex
Structure deposition date
2019-10-01
Thiol separation (Å)
6
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
92
Peptide accession
Q96Q15
Residue number A
798
Residue number B
802
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 798 of Serine/threonine-protein kinase SMG1

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 802 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 217 and 222. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
6l54
Structure name
structure of smg189
Structure deposition date
2019-10-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
38
Peptide accession
Q96Q15
Residue number A
217
Residue number B
222
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 217 of Serine/threonine-protein kinase SMG1

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 222 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 1842 and 1846. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6l53
Structure name
structure of smg1
Structure deposition date
2019-10-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
9
% buried
12
Peptide accession
Q96Q15
Residue number A
1842
Residue number B
1846
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 1842 of Serine/threonine-protein kinase SMG1

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 1846 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 296 and 299. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6l54
Structure name
structure of smg189
Structure deposition date
2019-10-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
30
Peptide accession
Q96Q15
Residue number A
296
Residue number B
299
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 296 of Serine/threonine-protein kinase SMG1

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 299 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 1023 and 1085. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6l53
Structure name
structure of smg1
Structure deposition date
2019-10-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
73
Peptide accession
Q96Q15
Residue number A
1023
Residue number B
1085
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 1023 of Serine/threonine-protein kinase SMG1

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 1085 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 489 and 492. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6l54
Structure name
structure of smg189
Structure deposition date
2019-10-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
75
Peptide accession
Q96Q15
Residue number A
489
Residue number B
492
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 489 of Serine/threonine-protein kinase SMG1

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 492 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 1023 and 1356. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6l54
Structure name
structure of smg189
Structure deposition date
2019-10-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
93
Peptide accession
Q96Q15
Residue number A
1023
Residue number B
1356
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 1023 of Serine/threonine-protein kinase SMG1

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 1356 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 761 and 798. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7pw7
Structure name
human smg1-9 kinase complex bound to a smg1 inhibitor
Structure deposition date
2021-10-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
11
% buried
80
Peptide accession
Q96Q15
Residue number A
761
Residue number B
798
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 761 of Serine/threonine-protein kinase SMG1

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 798 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 780 and 798. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
7pw9
Structure name
human smg1-9 kinase complex bound to amppnp
Structure deposition date
2021-10-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
78
Peptide accession
Q96Q15
Residue number A
780
Residue number B
798
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 780 of Serine/threonine-protein kinase SMG1

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 798 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 1081 and 1193. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
7pw5
Structure name
human smg1-8-9 kinase complex with alphafold predicted smg8 c- terminus, bound to a smg1 inhibitor
Structure deposition date
2021-10-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
96
Peptide accession
Q96Q15
Residue number A
1081
Residue number B
1193
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 1081 of Serine/threonine-protein kinase SMG1

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 1193 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 776 and 780. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
6syt
Structure name
structure of the smg1-smg8-smg9 complex
Structure deposition date
2019-10-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
71
Peptide accession
Q96Q15
Residue number A
776
Residue number B
780
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 776 of Serine/threonine-protein kinase SMG1

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 780 of Serine/threonine-protein kinase SMG1

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 Serine/threonine-protein kinase SMG1 between cysteines 1191 and 1193. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
7pw9
Structure name
human smg1-9 kinase complex bound to amppnp
Structure deposition date
2021-10-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
82
Peptide accession
Q96Q15
Residue number A
1191
Residue number B
1193
Peptide name
Serine/threonine-protein kinase SMG1

Ligandability

Cysteine 1191 of Serine/threonine-protein kinase SMG1

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 1193 of Serine/threonine-protein kinase SMG1

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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