ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase Mdm2

Intermolecular
Cysteine 449 and cysteine 449
Cysteine 478 and cysteine 461
Intramolecular
Cysteine 305 and cysteine 322
Cysteine 308 and cysteine 319
Cysteine 305 and cysteine 319
Cysteine 319 and cysteine 322
Cysteine 305 and cysteine 308
Cysteine 438 and cysteine 441
Cysteine 438 and cysteine 461
Cysteine 441 and cysteine 464
More...
Cysteine 441 and cysteine 461
Cysteine 308 and cysteine 322
Cysteine 461 and cysteine 464
Cysteine 438 and cysteine 464
Cysteine 475 and cysteine 478
Cysteine 449 and cysteine 475
A redox-regulated disulphide may form between two units of E3 ubiquitin-protein ligase Mdm2 at cysteines 449 and 449. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
6sqp
Structure name
crystal structure of cat mdm2-s429e ring domain homodimer
Structure deposition date
2019-09-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
100
Minimum pKa ?
12
% buried
100
Peptide A name
E3 ubiquitin-protein ligase Mdm2
Peptide B name
E3 ubiquitin-protein ligase Mdm2
Peptide A accession
Q7YRZ8
Peptide B accession
Q7YRZ8
Peptide A residue number
449
Peptide B residue number
449

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 E3 ubiquitin-protein ligase Mdm2 at cysteines 478 and 461. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
7tfg
Structure name
structure of mouse double minute 2 homolog (mdm2) ring domain in complex with ma242
Structure deposition date
2022-01-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
10
% buried
80
Peptide A name
E3 ubiquitin-protein ligase Mdm2
Peptide B name
E3 ubiquitin-protein ligase Mdm2
Peptide A accession
Q7YRZ8
Peptide B accession
Q7YRZ8
Peptide A residue number
478
Peptide B residue number
461

Ligandability

Cysteine 478 of E3 ubiquitin-protein ligase Mdm2

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 461 of E3 ubiquitin-protein ligase Mdm2

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 Mdm2 between cysteines 305 and 322.

Details

Redox score ?
89
PDB code
2c6a
Structure name
solution structure of the c4 zinc-finger domain of hdm2
Structure deposition date
2005-11-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
5
% buried
0
Peptide accession
Q00987
Residue number A
305
Residue number B
322
Peptide name
E3 ubiquitin-protein ligase Mdm2

Ligandability

Cysteine 305 of E3 ubiquitin-protein ligase Mdm2

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 E3 ubiquitin-protein ligase Mdm2

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 Mdm2 between cysteines 308 and 319.

Details

Redox score ?
89
PDB code
2c6b
Structure name
solution structure of the c4 zinc-finger domain of hdm2
Structure deposition date
2005-11-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
6
% buried
0
Peptide accession
Q00987
Residue number A
308
Residue number B
319
Peptide name
E3 ubiquitin-protein ligase Mdm2

Ligandability

Cysteine 308 of E3 ubiquitin-protein ligase Mdm2

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 319 of E3 ubiquitin-protein ligase Mdm2

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 Mdm2 between cysteines 305 and 319.

Details

Redox score ?
88
PDB code
2c6b
Structure name
solution structure of the c4 zinc-finger domain of hdm2
Structure deposition date
2005-11-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
6
% buried
0
Peptide accession
Q00987
Residue number A
305
Residue number B
319
Peptide name
E3 ubiquitin-protein ligase Mdm2

Ligandability

Cysteine 305 of E3 ubiquitin-protein ligase Mdm2

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 319 of E3 ubiquitin-protein ligase Mdm2

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 Mdm2 between cysteines 319 and 322.

Details

Redox score ?
87
PDB code
2c6b
Structure name
solution structure of the c4 zinc-finger domain of hdm2
Structure deposition date
2005-11-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
6
% buried
0
Peptide accession
Q00987
Residue number A
319
Residue number B
322
Peptide name
E3 ubiquitin-protein ligase Mdm2

Ligandability

Cysteine 319 of E3 ubiquitin-protein ligase Mdm2

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 E3 ubiquitin-protein ligase Mdm2

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 Mdm2 between cysteines 305 and 308.

Details

Redox score ?
86
PDB code
2c6b
Structure name
solution structure of the c4 zinc-finger domain of hdm2
Structure deposition date
2005-11-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
6
% buried
0
Peptide accession
Q00987
Residue number A
305
Residue number B
308
Peptide name
E3 ubiquitin-protein ligase Mdm2

Ligandability

Cysteine 305 of E3 ubiquitin-protein ligase Mdm2

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 308 of E3 ubiquitin-protein ligase Mdm2

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 Mdm2 between cysteines 438 and 441.

Details

Redox score ?
84
PDB code
2vje
Structure name
crystal structure of the mdm2-mdmx ring domain heterodimer
Structure deposition date
2007-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
7
% buried
8
Peptide accession
Q00987
Residue number A
438
Residue number B
441
Peptide name
E3 ubiquitin-protein ligase Mdm2

Ligandability

Cysteine 438 of E3 ubiquitin-protein ligase Mdm2

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 E3 ubiquitin-protein ligase Mdm2

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 Mdm2 between cysteines 438 and 461.

Details

Redox score ?
83
PDB code
2vje
Structure name
crystal structure of the mdm2-mdmx ring domain heterodimer
Structure deposition date
2007-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
5
% buried
16
Peptide accession
Q00987
Residue number A
438
Residue number B
461
Peptide name
E3 ubiquitin-protein ligase Mdm2

Ligandability

Cysteine 438 of E3 ubiquitin-protein ligase Mdm2

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 461 of E3 ubiquitin-protein ligase Mdm2

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 Mdm2 between cysteines 441 and 464.

Details

Redox score ?
78
PDB code
6sqo
Structure name
crystal structure of human mdm2 ring domain homodimer bound to ubch5b- ub
Structure deposition date
2019-09-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
4
% buried
52
Peptide accession
Q00987
Residue number A
441
Residue number B
464
Peptide name
E3 ubiquitin-protein ligase Mdm2

Ligandability

Cysteine 441 of E3 ubiquitin-protein ligase Mdm2

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 464 of E3 ubiquitin-protein ligase Mdm2

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 Mdm2 between cysteines 441 and 461.

Details

Redox score ?
78
PDB code
2vjf
Structure name
crystal structure of the mdm2-mdmx ring domain heterodimer
Structure deposition date
2007-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
7
% buried
20
Peptide accession
Q00987
Residue number A
441
Residue number B
461
Peptide name
E3 ubiquitin-protein ligase Mdm2

Ligandability

Cysteine 441 of E3 ubiquitin-protein ligase Mdm2

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 461 of E3 ubiquitin-protein ligase Mdm2

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 Mdm2 between cysteines 308 and 322.

Details

Redox score ?
78
PDB code
2c6a
Structure name
solution structure of the c4 zinc-finger domain of hdm2
Structure deposition date
2005-11-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
34
Minimum pKa ?
9
% buried
0
Peptide accession
Q00987
Residue number A
308
Residue number B
322
Peptide name
E3 ubiquitin-protein ligase Mdm2

Ligandability

Cysteine 308 of E3 ubiquitin-protein ligase Mdm2

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 E3 ubiquitin-protein ligase Mdm2

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 Mdm2 between cysteines 461 and 464.

Details

Redox score ?
76
PDB code
7t59
Structure name
structure of mouse double minute 2 homolog (mdm2) ring domain
Structure deposition date
2021-12-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
7
% buried
37
Peptide accession
Q7YRZ8
Residue number A
461
Residue number B
464
Peptide name
E3 ubiquitin-protein ligase Mdm2

Ligandability

Cysteine 461 of E3 ubiquitin-protein ligase Mdm2

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 464 of E3 ubiquitin-protein ligase Mdm2

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 Mdm2 between cysteines 438 and 464.

Details

Redox score ?
66
PDB code
6sqo
Structure name
crystal structure of human mdm2 ring domain homodimer bound to ubch5b- ub
Structure deposition date
2019-09-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
72
Peptide accession
Q00987
Residue number A
438
Residue number B
464
Peptide name
E3 ubiquitin-protein ligase Mdm2

Ligandability

Cysteine 438 of E3 ubiquitin-protein ligase Mdm2

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 464 of E3 ubiquitin-protein ligase Mdm2

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 Mdm2 between cysteines 475 and 478.

Details

Redox score ?
61
PDB code
5mnj
Structure name
structure of mdm2-mdmx-ubch5b-ubiquitin complex
Structure deposition date
2016-12-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
85
Minimum pKa ?
14
% buried
nan
Peptide accession
Q00987
Residue number A
475
Residue number B
478
Peptide name
E3 ubiquitin-protein ligase Mdm2

Ligandability

Cysteine 475 of E3 ubiquitin-protein ligase Mdm2

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 478 of E3 ubiquitin-protein ligase Mdm2

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 Mdm2 between cysteines 449 and 475. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
7thl
Structure name
structure of mouse double minute 2 homolog (mdm2) ring domain in complex with inulanolide a
Structure deposition date
2022-01-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
10
% buried
76
Peptide accession
Q7YRZ8
Residue number A
449
Residue number B
475
Peptide name
E3 ubiquitin-protein ligase Mdm2

Ligandability

Cysteine 449 of E3 ubiquitin-protein ligase Mdm2

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 475 of E3 ubiquitin-protein ligase Mdm2

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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