ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Actin-related protein 2/3 complex subunit 3

Intramolecular
Cysteine 85 and cysteine 145
Cysteine 78 and cysteine 145
Cysteine 78 and cysteine 85
A redox-regulated disulphide may form within Actin-related protein 2/3 complex subunit 3 between cysteines 85 and 145. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
4xf2
Structure name
tetragonal structure of arp2/3 complex
Structure deposition date
2014-12-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
11
% buried
46
Peptide accession
Q3T035
Residue number A
85
Residue number B
145
Peptide name
Actin-related protein 2/3 complex subunit 3

Ligandability

Cysteine 85 of Actin-related protein 2/3 complex subunit 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 145 of Actin-related protein 2/3 complex subunit 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 Actin-related protein 2/3 complex subunit 3 between cysteines 78 and 145. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
4jd2
Structure name
crystal structure of bos taurus arp2/3 complex binding with mus musculus gmf
Structure deposition date
2013-02-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
72
Peptide accession
Q3T035
Residue number A
78
Residue number B
145
Peptide name
Actin-related protein 2/3 complex subunit 3

Ligandability

Cysteine 78 of Actin-related protein 2/3 complex subunit 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 145 of Actin-related protein 2/3 complex subunit 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 Actin-related protein 2/3 complex subunit 3 between cysteines 78 and 85. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
4xf2
Structure name
tetragonal structure of arp2/3 complex
Structure deposition date
2014-12-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
59
Peptide accession
Q3T035
Residue number A
78
Residue number B
85
Peptide name
Actin-related protein 2/3 complex subunit 3

Ligandability

Cysteine 78 of Actin-related protein 2/3 complex subunit 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 85 of Actin-related protein 2/3 complex subunit 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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