ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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M-phase inducer phosphatase 3

Intramolecular
Cysteine 330 and cysteine 377
Cysteine 388 and cysteine 390
Cysteine 330 and cysteine 388
A redox-regulated disulphide may form within M-phase inducer phosphatase 3 between cysteines 330 and 377. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
3op3
Structure name
crystal structure of cell division cycle 25c protein isoform a from homo sapiens
Structure deposition date
2010-08-31
Thiol separation (Å)
6
Half-sphere exposure sum ?
78
Minimum pKa ?
9
% buried
89
Peptide accession
P30307
Residue number A
330
Residue number B
377
Peptide name
M-phase inducer phosphatase 3

Ligandability

Cysteine 330 of M-phase inducer phosphatase 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 377 of M-phase inducer phosphatase 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.

A redox-regulated disulphide may form within M-phase inducer phosphatase 3 between cysteines 388 and 390. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
3op3
Structure name
crystal structure of cell division cycle 25c protein isoform a from homo sapiens
Structure deposition date
2010-08-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
56
Peptide accession
P30307
Residue number A
388
Residue number B
390
Peptide name
M-phase inducer phosphatase 3

Ligandability

Cysteine 388 of M-phase inducer phosphatase 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 390 of M-phase inducer phosphatase 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.

A redox-regulated disulphide may form within M-phase inducer phosphatase 3 between cysteines 330 and 388. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
3op3
Structure name
crystal structure of cell division cycle 25c protein isoform a from homo sapiens
Structure deposition date
2010-08-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
95
Peptide accession
P30307
Residue number A
330
Residue number B
388
Peptide name
M-phase inducer phosphatase 3

Ligandability

Cysteine 330 of M-phase inducer phosphatase 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 388 of M-phase inducer phosphatase 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.

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