ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Protein cereblon

Intermolecular
Cysteine 99 of Tumor suppressor candidate 3 and cysteine 234
Cysteine 346 and cysteine 325
Cysteine 329 and cysteine 397
Cysteine 346 and cysteine 329
Cysteine 394 and cysteine 329
Cysteine 326 and cysteine 329
Cysteine 329 and cysteine 329
Cysteine 397 and cysteine 397
Cysteine 397 and cysteine 394
Cysteine 326 and cysteine 397
More...
Intramolecular
Cysteine 326 and cysteine 394
Cysteine 323 and cysteine 391
Cysteine 323 and cysteine 326
Cysteine 326 and cysteine 391
Cysteine 323 and cysteine 394
Cysteine 391 and cysteine 394
Cysteine 322 and cysteine 326
Cysteine 318 and cysteine 441
Cysteine 322 and cysteine 323
Cysteine 322 and cysteine 394
Cysteine 322 and cysteine 391
Cysteine 318 and cysteine 322
Cysteine 366 and cysteine 391
Cysteine 287 and cysteine 343 L
Cysteine 322 and cysteine 366
Cysteine 310 and cysteine 441
Cysteine 310 and cysteine 318
Cysteine 205 and cysteine 234
A redox-regulated disulphide may form between cysteine 99 of Tumor suppressor candidate 3 and cysteine 234 of Protein cereblon (58 and 6 respectively in this structure).

Details

Redox score ?
90
PDB code
4m91
Structure name
crystal structure of hn33/tusc3-peptide 1
Structure deposition date
2013-08-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide A name
Tumor suppressor candidate 3
Peptide B name
Protein cereblon
Peptide A accession
Q13454
Peptide B accession
Q96SW2
Peptide A residue number
99
Peptide B residue number
234

Ligandability

Cysteine 99 of Tumor suppressor candidate 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 234 of Protein cereblon

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 between two units of Protein cereblon at cysteines 346 and 325.

Details

Redox score ?
70
PDB code
5yiz
Structure name
mouse cereblon thalidomide binding domain complexed with racemic thalidomide
Structure deposition date
2017-10-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
26
Peptide A name
Protein cereblon
Peptide B name
Protein cereblon
Peptide A accession
Q8C7D2
Peptide B accession
Q8C7D2
Peptide A residue number
346
Peptide B residue number
325

Ligandability

Cysteine 346 of Protein cereblon

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 325 of Protein cereblon

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 between two units of Protein cereblon at cysteines 329 and 397.

Details

Redox score ?
63
PDB code
5yj0
Structure name
mouse cereblon thalidomide binding domain complexed with s-form thalidomide
Structure deposition date
2017-10-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
6
% buried
52
Peptide A name
Protein cereblon
Peptide B name
Protein cereblon
Peptide A accession
Q8C7D2
Peptide B accession
Q8C7D2
Peptide A residue number
329
Peptide B residue number
397

Ligandability

Cysteine 329 of Protein cereblon

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 Protein cereblon

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 between two units of Protein cereblon at cysteines 346 and 329. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
5yj1
Structure name
mouse cereblon thalidomide binding domain complexed with r-form thalidomide
Structure deposition date
2017-10-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
5
% buried
46
Peptide A name
Protein cereblon
Peptide B name
Protein cereblon
Peptide A accession
Q8C7D2
Peptide B accession
Q8C7D2
Peptide A residue number
346
Peptide B residue number
329

Ligandability

Cysteine 346 of Protein cereblon

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 329 of Protein cereblon

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 between two units of Protein cereblon at cysteines 394 and 329. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
5yj0
Structure name
mouse cereblon thalidomide binding domain complexed with s-form thalidomide
Structure deposition date
2017-10-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
6
% buried
54
Peptide A name
Protein cereblon
Peptide B name
Protein cereblon
Peptide A accession
Q8C7D2
Peptide B accession
Q8C7D2
Peptide A residue number
394
Peptide B residue number
329

Ligandability

Cysteine 394 of Protein cereblon

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 329 of Protein cereblon

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 between two units of Protein cereblon at cysteines 326 and 329. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
5yj1
Structure name
mouse cereblon thalidomide binding domain complexed with r-form thalidomide
Structure deposition date
2017-10-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
5
% buried
66
Peptide A name
Protein cereblon
Peptide B name
Protein cereblon
Peptide A accession
Q8C7D2
Peptide B accession
Q8C7D2
Peptide A residue number
326
Peptide B residue number
329

Ligandability

Cysteine 326 of Protein cereblon

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 329 of Protein cereblon

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 between two units of Protein cereblon at cysteines 329 and 329. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
5yiz
Structure name
mouse cereblon thalidomide binding domain complexed with racemic thalidomide
Structure deposition date
2017-10-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
14
% buried
nan
Peptide A name
Protein cereblon
Peptide B name
Protein cereblon
Peptide A accession
Q8C7D2
Peptide B accession
Q8C7D2
Peptide A residue number
329
Peptide B residue number
329

Ligandability

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 between two units of Protein cereblon at cysteines 397 and 397. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
5yiz
Structure name
mouse cereblon thalidomide binding domain complexed with racemic thalidomide
Structure deposition date
2017-10-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
12
% buried
50
Peptide A name
Protein cereblon
Peptide B name
Protein cereblon
Peptide A accession
Q8C7D2
Peptide B accession
Q8C7D2
Peptide A residue number
397
Peptide B residue number
397

Ligandability

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 between two units of Protein cereblon at cysteines 397 and 394. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
5yj1
Structure name
mouse cereblon thalidomide binding domain complexed with r-form thalidomide
Structure deposition date
2017-10-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
14
% buried
68
Peptide A name
Protein cereblon
Peptide B name
Protein cereblon
Peptide A accession
Q8C7D2
Peptide B accession
Q8C7D2
Peptide A residue number
397
Peptide B residue number
394

Ligandability

Cysteine 397 of Protein cereblon

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 394 of Protein cereblon

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 between two units of Protein cereblon at cysteines 326 and 397. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
9
PDB code
5yiz
Structure name
mouse cereblon thalidomide binding domain complexed with racemic thalidomide
Structure deposition date
2017-10-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
22
% buried
67
Peptide A name
Protein cereblon
Peptide B name
Protein cereblon
Peptide A accession
Q8C7D2
Peptide B accession
Q8C7D2
Peptide A residue number
326
Peptide B residue number
397

Ligandability

Cysteine 326 of Protein cereblon

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 Protein cereblon

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 Protein cereblon between cysteines 326 and 394.

Details

Redox score ?
86
PDB code
6h0g
Structure name
structure of the ddb1-crbn-pomalidomide complex bound to znf692(zf4)
Structure deposition date
2018-07-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
20
Peptide accession
Q96SW2
Residue number A
326
Residue number B
394
Peptide name
Protein cereblon

Ligandability

Cysteine 326 of Protein cereblon

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 394 of Protein cereblon

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 Protein cereblon between cysteines 323 and 391.

Details

Redox score ?
84
PDB code
5v3o
Structure name
cereblon in complex with ddb1 and cc-220
Structure deposition date
2017-03-07
Thiol separation (Å)
3
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
14
Peptide accession
Q96SW2
Residue number A
323
Residue number B
391
Peptide name
Protein cereblon

Ligandability

Cysteine 323 of Protein cereblon

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 391 of Protein cereblon

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 Protein cereblon between cysteines 323 and 326.

Details

Redox score ?
84
PDB code
5hxb
Structure name
cereblon in complex with ddb1, cc-885, and gspt1
Structure deposition date
2016-01-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
8
Peptide accession
Q96SW2
Residue number A
323
Residue number B
326
Peptide name
Protein cereblon

Ligandability

Cysteine 323 of Protein cereblon

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 326 of Protein cereblon

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 Protein cereblon between cysteines 326 and 391.

Details

Redox score ?
84
PDB code
5v3o
Structure name
cereblon in complex with ddb1 and cc-220
Structure deposition date
2017-03-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
7
% buried
4
Peptide accession
Q96SW2
Residue number A
326
Residue number B
391
Peptide name
Protein cereblon

Ligandability

Cysteine 326 of Protein cereblon

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 391 of Protein cereblon

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 Protein cereblon between cysteines 323 and 394.

Details

Redox score ?
83
PDB code
5hxb
Structure name
cereblon in complex with ddb1, cc-885, and gspt1
Structure deposition date
2016-01-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
57
Minimum pKa ?
6
% buried
nan
Peptide accession
Q96SW2
Residue number A
323
Residue number B
394
Peptide name
Protein cereblon

Ligandability

Cysteine 323 of Protein cereblon

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 394 of Protein cereblon

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 Protein cereblon between cysteines 391 and 394.

Details

Redox score ?
78
PDB code
5hxb
Structure name
cereblon in complex with ddb1, cc-885, and gspt1
Structure deposition date
2016-01-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
nan
Peptide accession
Q96SW2
Residue number A
391
Residue number B
394
Peptide name
Protein cereblon

Ligandability

Cysteine 391 of Protein cereblon

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 394 of Protein cereblon

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 Protein cereblon between cysteines 322 and 326. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
6bnb
Structure name
crystal structure of ddb1-crbn-brd4(bd1) complex bound to dbet57 protac
Structure deposition date
2017-11-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
10
Peptide accession
Q96SW2
Residue number A
322
Residue number B
326
Peptide name
Protein cereblon

Ligandability

Cysteine 322 of Protein cereblon

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 326 of Protein cereblon

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 Protein cereblon between cysteines 318 and 441. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
6h0g
Structure name
structure of the ddb1-crbn-pomalidomide complex bound to znf692(zf4)
Structure deposition date
2018-07-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
69
Peptide accession
Q96SW2
Residue number A
318
Residue number B
441
Peptide name
Protein cereblon

Ligandability

Cysteine 318 of Protein cereblon

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 441 of Protein cereblon

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 Protein cereblon between cysteines 322 and 323. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
5hxb
Structure name
cereblon in complex with ddb1, cc-885, and gspt1
Structure deposition date
2016-01-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
6
% buried
28
Peptide accession
Q96SW2
Residue number A
322
Residue number B
323
Peptide name
Protein cereblon

Ligandability

Cysteine 322 of Protein cereblon

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 323 of Protein cereblon

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 Protein cereblon between cysteines 322 and 394. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
8d80
Structure name
cereblon~ddb1 bound to iberdomide and ikaros zf1-2-3
Structure deposition date
2022-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
8
Peptide accession
Q96SW2
Residue number A
322
Residue number B
394
Peptide name
Protein cereblon

Ligandability

Cysteine 322 of Protein cereblon

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 394 of Protein cereblon

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 Protein cereblon between cysteines 322 and 391. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6boy
Structure name
crystal structure of ddb1-crbn-brd4(bd1) complex bound to dbet6 protac
Structure deposition date
2017-11-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
8
% buried
19
Peptide accession
Q96SW2
Residue number A
322
Residue number B
391
Peptide name
Protein cereblon

Ligandability

Cysteine 322 of Protein cereblon

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 391 of Protein cereblon

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 Protein cereblon between cysteines 318 and 322. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
5hxb
Structure name
cereblon in complex with ddb1, cc-885, and gspt1
Structure deposition date
2016-01-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
48
Peptide accession
Q96SW2
Residue number A
318
Residue number B
322
Peptide name
Protein cereblon

Ligandability

Cysteine 318 of Protein cereblon

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 322 of Protein cereblon

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 Protein cereblon between cysteines 366 and 391. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
5fqd
Structure name
structural basis of lenalidomide induced ck1a degradation by the crl4crbn ubiquitin ligase
Structure deposition date
2015-12-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
8
% buried
24
Peptide accession
Q96SW2
Residue number A
366
Residue number B
391
Peptide name
Protein cereblon

Ligandability

Cysteine 366 of Protein cereblon

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 391 of Protein cereblon

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 Protein cereblon between cysteines 287 and 343. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6xk9
Structure name
cereblon in complex with ddb1, cc-90009, and gspt1
Structure deposition date
2020-06-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
10
% buried
96
Peptide accession
Q96SW2
Residue number A
287
Residue number B
343
Peptide name
Protein cereblon

Ligandability

Cysteine 287 of Protein cereblon

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.

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 343 of Protein cereblon

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 Protein cereblon between cysteines 322 and 366. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
5fqd
Structure name
structural basis of lenalidomide induced ck1a degradation by the crl4crbn ubiquitin ligase
Structure deposition date
2015-12-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
32
Peptide accession
Q96SW2
Residue number A
322
Residue number B
366
Peptide name
Protein cereblon

Ligandability

Cysteine 322 of Protein cereblon

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 366 of Protein cereblon

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 Protein cereblon between cysteines 310 and 441. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6h0g
Structure name
structure of the ddb1-crbn-pomalidomide complex bound to znf692(zf4)
Structure deposition date
2018-07-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
92
Peptide accession
Q96SW2
Residue number A
310
Residue number B
441
Peptide name
Protein cereblon

Ligandability

Cysteine 310 of Protein cereblon

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 441 of Protein cereblon

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 Protein cereblon between cysteines 310 and 318. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6uml
Structure name
structural basis for thalidomide teratogenicity revealed by the cereblon-ddb1-sall4-pomalidomide complex
Structure deposition date
2019-10-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
59
Peptide accession
Q96SW2
Residue number A
310
Residue number B
318
Peptide name
Protein cereblon

Ligandability

Cysteine 310 of Protein cereblon

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 318 of Protein cereblon

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 Protein cereblon between cysteines 205 and 234. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6h0f
Structure name
structure of ddb1-crbn-pomalidomide complex bound to ikzf1(zf2)
Structure deposition date
2018-07-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
100
Peptide accession
Q96SW2
Residue number A
205
Residue number B
234
Peptide name
Protein cereblon

Ligandability

Cysteine 205 of Protein cereblon

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 234 of Protein cereblon

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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