ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Filamin-B

Intramolecular
Cysteine 1868 and cysteine 1876
Cysteine 1375 and cysteine 1383
Cysteine 1087 and cysteine 1095 L
Cysteine 2115 and cysteine 2154 L
Cysteine 178 and cysteine 183
A redox-regulated disulphide may form within Filamin-B between cysteines 1868 and 1876.

Details

Redox score ?
77
PDB code
5dcp
Structure name
crystal structure of the human filamin b ig-like domains 16-17
Structure deposition date
2015-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
19
Peptide accession
O75369
Residue number A
1868
Residue number B
1876
Peptide name
Filamin-B

Ligandability

Cysteine 1868 of Filamin-B

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 1876 of Filamin-B

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 Filamin-B between cysteines 1375 and 1383 (58 and 66 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
2dic
Structure name
solution structure of the 12th filamin domain from human filamin-b
Structure deposition date
2006-03-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
50
Minimum pKa ?
10
% buried
19
Peptide accession
O75369
Residue number A
1375
Residue number B
1383
Peptide name
Filamin-B

Ligandability

Cysteine 1375 of Filamin-B

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 1383 of Filamin-B

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 Filamin-B between cysteines 1087 and 1095 (78 and 86 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
2di9
Structure name
solution structure of the 9th filamin domain from human filamin-b
Structure deposition date
2006-03-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
12
Peptide accession
O75369
Residue number A
1087
Residue number B
1095
Peptide name
Filamin-B

Ligandability

Cysteine 1087 of Filamin-B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

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 1095 of Filamin-B

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 Filamin-B between cysteines 2115 and 2154 (29 and 68 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2e9i
Structure name
solution structure of the n-terminal extended 20th filamin domain from human filamin-b
Structure deposition date
2007-01-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
46
Minimum pKa ?
10
% buried
10
Peptide accession
O75369
Residue number A
2115
Residue number B
2154
Peptide name
Filamin-B

Ligandability

Cysteine 2115 of Filamin-B

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2154 of Filamin-B

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 Filamin-B between cysteines 178 and 183. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2wa6
Structure name
structure of the w148r mutant of human filamin b actin binding domain at 1
Structure deposition date
2009-02-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
55
Peptide accession
O75369
Residue number A
178
Residue number B
183
Peptide name
Filamin-B

Ligandability

Cysteine 178 of Filamin-B

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 183 of Filamin-B

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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