ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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F-BAR domain only protein 2

Intermolecular
Cysteine 147 and cysteine 810
Cysteine 273 and cysteine 147
Intramolecular
Cysteine 212 and cysteine 251
A redox-regulated disulphide may form between two units of F-BAR domain only protein 2 at cysteines 147 and 810 (147 and 273 respectively in this structure).

Details

Redox score ?
88
PDB code
2v0o
Structure name
fcho2 f-bar domain
Structure deposition date
2007-05-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
F-BAR domain only protein 2
Peptide B name
F-BAR domain only protein 2
Peptide A accession
Q96CF5
Peptide B accession
Q96CF5
Peptide A residue number
147
Peptide B residue number
810

Ligandability

Cysteine 147 of F-BAR domain only protein 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 810 of F-BAR domain only protein 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 between two units of F-BAR domain only protein 2 at cysteines 273 and 147.

Details

Redox score ?
87
PDB code
2v0o
Structure name
fcho2 f-bar domain
Structure deposition date
2007-05-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide A name
F-BAR domain only protein 2
Peptide B name
F-BAR domain only protein 2
Peptide A accession
Q96CF5
Peptide B accession
Q96CF5
Peptide A residue number
273
Peptide B residue number
147

Ligandability

Cysteine 273 of F-BAR domain only protein 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 147 of F-BAR domain only protein 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 F-BAR domain only protein 2 between cysteines 212 and 251.

Details

Redox score ?
nan
PDB code
7ohz
Structure name
crystal structure of ap2 mu2 - fcho2 chimera (his6-tagged)
Structure deposition date
2021-05-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
12
% buried
82
Peptide accession
Q0JRZ9
Residue number A
212
Residue number B
251
Peptide name
F-BAR domain only protein 2

Ligandability

Cysteine 212 of F-BAR domain only protein 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 251 of F-BAR domain only protein 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 212 in protein A could not be asigned to a Uniprot residue.
Cysteine 251 in protein B could not be asigned to a Uniprot residue.
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