ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Beta-arrestin-2

Intermolecular
Cysteine 244 and cysteine 244
Intramolecular
Cysteine 141 and cysteine 244 L
Cysteine 60 and cysteine 126
A redox-regulated disulphide may form between two units of Beta-arrestin-2 at cysteines 244 and 244. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6k3f
Structure name
crystal structure of beta-arrestin 2 in complex with cxcr7 phosphopeptide
Structure deposition date
2019-05-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
12
% buried
72
Peptide A name
Beta-arrestin-2
Peptide B name
Beta-arrestin-2
Peptide A accession
P29067
Peptide B accession
P29067
Peptide A residue number
244
Peptide B residue number
244

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 within Beta-arrestin-2 between cysteines 141 and 244. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6k3f
Structure name
crystal structure of beta-arrestin 2 in complex with cxcr7 phosphopeptide
Structure deposition date
2019-05-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
65
Peptide accession
P29067
Residue number A
141
Residue number B
244
Peptide name
Beta-arrestin-2

Ligandability

Cysteine 141 of Beta-arrestin-2

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 244 of Beta-arrestin-2

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 Beta-arrestin-2 between cysteines 60 and 126. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
3p2d
Structure name
crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes
Structure deposition date
2010-10-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
11
% buried
93
Peptide accession
P32120
Residue number A
60
Residue number B
126
Peptide name
Beta-arrestin-2

Ligandability

Cysteine 60 of Beta-arrestin-2

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 126 of Beta-arrestin-2

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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