ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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M-phase inducer phosphatase 1

Intramolecular
Cysteine 477 and cysteine 481
Cysteine 385 and cysteine 431
Cysteine 385 and cysteine 442
A redox-regulated disulphide may form within M-phase inducer phosphatase 1 between cysteines 477 and 481 (476 and 480 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
1c25
Structure name
human cdc25a catalytic domain
Structure deposition date
1998-04-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
38
Peptide accession
P30304
Residue number A
477
Residue number B
481
Peptide name
M-phase inducer phosphatase 1

Ligandability

Cysteine 477 of M-phase inducer phosphatase 1

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 481 of M-phase inducer phosphatase 1

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 1 between cysteines 385 and 431 (384 and 430 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
1c25
Structure name
human cdc25a catalytic domain
Structure deposition date
1998-04-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
83
Minimum pKa ?
11
% buried
88
Peptide accession
P30304
Residue number A
385
Residue number B
431
Peptide name
M-phase inducer phosphatase 1

Ligandability

Cysteine 385 of M-phase inducer phosphatase 1

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 431 of M-phase inducer phosphatase 1

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 1 between cysteines 385 and 442 (384 and 441 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
1c25
Structure name
human cdc25a catalytic domain
Structure deposition date
1998-04-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
98
Peptide accession
P30304
Residue number A
385
Residue number B
442
Peptide name
M-phase inducer phosphatase 1

Ligandability

Cysteine 385 of M-phase inducer phosphatase 1

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 442 of M-phase inducer phosphatase 1

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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