ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase HUWE1

Intermolecular
Cysteine 4341 and cysteine 229 of Polyubiquitin-B L
Intramolecular
Cysteine 467 and cysteine 500
Cysteine 1879 and cysteine 2655
Cysteine 1762 and cysteine 1782
Cysteine 1159 and cysteine 1421
Cysteine 1891 and cysteine 1892 L
Cysteine 467 and cysteine 471
Cysteine 1879 and cysteine 2666
Cysteine 182 and cysteine 183
Cysteine 471 and cysteine 500
More...
Cysteine 2655 and cysteine 2666
Cysteine 612 and cysteine 624
Cysteine 3635 and cysteine 3863
Cysteine 1278 and cysteine 1447
Cysteine 1278 and cysteine 1462
Cysteine 942 and cysteine 1133
Cysteine 821 and cysteine 828
Cysteine 1462 and cysteine 1544
A redox-regulated disulphide may form between cysteine 4341 of E3 ubiquitin-protein ligase HUWE1 and cysteine 229 of Polyubiquitin-B (352 and 76 respectively in this structure).

Details

Redox score ?
86
PDB code
6fyh
Structure name
disulfide between ubiquitin g76c and the e3 hect ligase huwe1
Structure deposition date
2018-03-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
E3 ubiquitin-protein ligase HUWE1
Peptide B name
Polyubiquitin-B
Peptide A accession
Q7Z6Z7
Peptide B accession
P0CG47
Peptide A residue number
4341
Peptide B residue number
229

Ligandability

Cysteine 4341 of E3 ubiquitin-protein ligase HUWE1

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.

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 229 of Polyubiquitin-B

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 E3 ubiquitin-protein ligase HUWE1 between cysteines 467 and 500.

Details

Redox score ?
82
PDB code
7jq9
Structure name
cryo-em structure of human huwe1
Structure deposition date
2020-08-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
7
% buried
66
Peptide accession
Q7Z6Z7
Residue number A
467
Residue number B
500
Peptide name
E3 ubiquitin-protein ligase HUWE1

Ligandability

Cysteine 467 of E3 ubiquitin-protein ligase HUWE1

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 500 of E3 ubiquitin-protein ligase HUWE1

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 E3 ubiquitin-protein ligase HUWE1 between cysteines 1879 and 2655.

Details

Redox score ?
68
PDB code
7mwf
Structure name
huwe1 in map with focus on interface
Structure deposition date
2021-05-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
90
Peptide accession
Q7Z6Z7
Residue number A
1879
Residue number B
2655
Peptide name
E3 ubiquitin-protein ligase HUWE1

Ligandability

Cysteine 1879 of E3 ubiquitin-protein ligase HUWE1

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 2655 of E3 ubiquitin-protein ligase HUWE1

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 E3 ubiquitin-protein ligase HUWE1 between cysteines 1762 and 1782.

Details

Redox score ?
66
PDB code
7mwd
Structure name
huwe1 in map with focus on hect
Structure deposition date
2021-05-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
91
Minimum pKa ?
9
% buried
100
Peptide accession
Q7Z6Z7
Residue number A
1762
Residue number B
1782
Peptide name
E3 ubiquitin-protein ligase HUWE1

Ligandability

Cysteine 1762 of E3 ubiquitin-protein ligase HUWE1

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 1782 of E3 ubiquitin-protein ligase HUWE1

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 E3 ubiquitin-protein ligase HUWE1 between cysteines 1159 and 1421.

Details

Redox score ?
64
PDB code
7mop
Structure name
cryo-em structure of human huwe1 in complex with ddit4
Structure deposition date
2021-05-03
Thiol separation (Å)
6
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
24
Peptide accession
Q7Z6Z7
Residue number A
1159
Residue number B
1421
Peptide name
E3 ubiquitin-protein ligase HUWE1

Ligandability

Cysteine 1159 of E3 ubiquitin-protein ligase HUWE1

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 1421 of E3 ubiquitin-protein ligase HUWE1

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 E3 ubiquitin-protein ligase HUWE1 between cysteines 1891 and 1892. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
7mwe
Structure name
huwe1 in map with focus on wwe
Structure deposition date
2021-05-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
34
Peptide accession
Q7Z6Z7
Residue number A
1891
Residue number B
1892
Peptide name
E3 ubiquitin-protein ligase HUWE1

Ligandability

Cysteine 1891 of E3 ubiquitin-protein ligase HUWE1

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 1892 of E3 ubiquitin-protein ligase HUWE1

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 E3 ubiquitin-protein ligase HUWE1 between cysteines 467 and 471. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
7mop
Structure name
cryo-em structure of human huwe1 in complex with ddit4
Structure deposition date
2021-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
6
% buried
40
Peptide accession
Q7Z6Z7
Residue number A
467
Residue number B
471
Peptide name
E3 ubiquitin-protein ligase HUWE1

Ligandability

Cysteine 467 of E3 ubiquitin-protein ligase HUWE1

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 471 of E3 ubiquitin-protein ligase HUWE1

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 E3 ubiquitin-protein ligase HUWE1 between cysteines 1879 and 2666. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
7jq9
Structure name
cryo-em structure of human huwe1
Structure deposition date
2020-08-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
14
% buried
96
Peptide accession
Q7Z6Z7
Residue number A
1879
Residue number B
2666
Peptide name
E3 ubiquitin-protein ligase HUWE1

Ligandability

Cysteine 1879 of E3 ubiquitin-protein ligase HUWE1

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 2666 of E3 ubiquitin-protein ligase HUWE1

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 E3 ubiquitin-protein ligase HUWE1 between cysteines 182 and 183. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
7mwd
Structure name
huwe1 in map with focus on hect
Structure deposition date
2021-05-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
96
Peptide accession
Q7Z6Z7
Residue number A
182
Residue number B
183
Peptide name
E3 ubiquitin-protein ligase HUWE1

Ligandability

Cysteine 182 of E3 ubiquitin-protein ligase HUWE1

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 183 of E3 ubiquitin-protein ligase HUWE1

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 E3 ubiquitin-protein ligase HUWE1 between cysteines 471 and 500. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
7mop
Structure name
cryo-em structure of human huwe1 in complex with ddit4
Structure deposition date
2021-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
49
Minimum pKa ?
10
% buried
36
Peptide accession
Q7Z6Z7
Residue number A
471
Residue number B
500
Peptide name
E3 ubiquitin-protein ligase HUWE1

Ligandability

Cysteine 471 of E3 ubiquitin-protein ligase HUWE1

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 500 of E3 ubiquitin-protein ligase HUWE1

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 E3 ubiquitin-protein ligase HUWE1 between cysteines 2655 and 2666. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
7mwe
Structure name
huwe1 in map with focus on wwe
Structure deposition date
2021-05-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
83
Peptide accession
Q7Z6Z7
Residue number A
2655
Residue number B
2666
Peptide name
E3 ubiquitin-protein ligase HUWE1

Ligandability

Cysteine 2655 of E3 ubiquitin-protein ligase HUWE1

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 2666 of E3 ubiquitin-protein ligase HUWE1

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 E3 ubiquitin-protein ligase HUWE1 between cysteines 612 and 624. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
7mwe
Structure name
huwe1 in map with focus on wwe
Structure deposition date
2021-05-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
60
Peptide accession
Q7Z6Z7
Residue number A
612
Residue number B
624
Peptide name
E3 ubiquitin-protein ligase HUWE1

Ligandability

Cysteine 612 of E3 ubiquitin-protein ligase HUWE1

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 624 of E3 ubiquitin-protein ligase HUWE1

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 E3 ubiquitin-protein ligase HUWE1 between cysteines 3635 and 3863. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
7mwe
Structure name
huwe1 in map with focus on wwe
Structure deposition date
2021-05-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
59
Peptide accession
Q7Z6Z7
Residue number A
3635
Residue number B
3863
Peptide name
E3 ubiquitin-protein ligase HUWE1

Ligandability

Cysteine 3635 of E3 ubiquitin-protein ligase HUWE1

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 3863 of E3 ubiquitin-protein ligase HUWE1

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 E3 ubiquitin-protein ligase HUWE1 between cysteines 1278 and 1447. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
7mop
Structure name
cryo-em structure of human huwe1 in complex with ddit4
Structure deposition date
2021-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
96
Peptide accession
Q7Z6Z7
Residue number A
1278
Residue number B
1447
Peptide name
E3 ubiquitin-protein ligase HUWE1

Ligandability

Cysteine 1278 of E3 ubiquitin-protein ligase HUWE1

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 1447 of E3 ubiquitin-protein ligase HUWE1

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 E3 ubiquitin-protein ligase HUWE1 between cysteines 1278 and 1462. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
7mwd
Structure name
huwe1 in map with focus on hect
Structure deposition date
2021-05-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
80
Peptide accession
Q7Z6Z7
Residue number A
1278
Residue number B
1462
Peptide name
E3 ubiquitin-protein ligase HUWE1

Ligandability

Cysteine 1278 of E3 ubiquitin-protein ligase HUWE1

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 1462 of E3 ubiquitin-protein ligase HUWE1

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 E3 ubiquitin-protein ligase HUWE1 between cysteines 942 and 1133. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
7jq9
Structure name
cryo-em structure of human huwe1
Structure deposition date
2020-08-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
92
Peptide accession
Q7Z6Z7
Residue number A
942
Residue number B
1133
Peptide name
E3 ubiquitin-protein ligase HUWE1

Ligandability

Cysteine 942 of E3 ubiquitin-protein ligase HUWE1

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 1133 of E3 ubiquitin-protein ligase HUWE1

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 E3 ubiquitin-protein ligase HUWE1 between cysteines 821 and 828. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
7jq9
Structure name
cryo-em structure of human huwe1
Structure deposition date
2020-08-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
95
Minimum pKa ?
12
% buried
100
Peptide accession
Q7Z6Z7
Residue number A
821
Residue number B
828
Peptide name
E3 ubiquitin-protein ligase HUWE1

Ligandability

Cysteine 821 of E3 ubiquitin-protein ligase HUWE1

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 828 of E3 ubiquitin-protein ligase HUWE1

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 E3 ubiquitin-protein ligase HUWE1 between cysteines 1462 and 1544. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
7jq9
Structure name
cryo-em structure of human huwe1
Structure deposition date
2020-08-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
13
% buried
87
Peptide accession
Q7Z6Z7
Residue number A
1462
Residue number B
1544
Peptide name
E3 ubiquitin-protein ligase HUWE1

Ligandability

Cysteine 1462 of E3 ubiquitin-protein ligase HUWE1

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 1544 of E3 ubiquitin-protein ligase HUWE1

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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