a tool for identifying drug-targetable redox-active disulphides

Filamin-C

Intermolecular

Cysteine 712 and cysteine 712

Cysteine 1653 and cysteine 1653

Intramolecular

Cysteine 618 and cysteine 626 L

Cysteine 1906 and cysteine 1914

Cysteine 2552 and cysteine 2555

A redox-regulated disulphide may form between two units of Filamin-C at cysteines 712 and 712.

Details

Redox score ?

79

PDB code

Structure name

human filamin c ig - like domains 4 and 5

Structure deposition date

2011-12-23

Thiol separation (Å)

3

Half-sphere exposure sum ?

59

Minimum pK_a ?

8

% buried

66

Peptide A name

Filamin-C

Peptide B name

Filamin-C

Peptide A accession

Peptide B accession

Peptide A residue number

712

Peptide B residue number

712

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 between two units of Filamin-C at cysteines 1653 and 1653.

Details

Redox score ?

78

PDB code

Structure name

crystal structure of human filamin c domains 14-15 cardiovascular disease causing mutation g1676r

Structure deposition date

2021-06-29

Thiol separation (Å)

2

Half-sphere exposure sum ?

76

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Filamin-C

Peptide B name

Filamin-C

Peptide A accession

Peptide B accession

Peptide A residue number

1653

Peptide B residue number

1653

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 Filamin-C between cysteines 618 and 626.

Details

Redox score ?

76

PDB code

Structure name

human filamin c ig - like domains 4 and 5

Structure deposition date

2011-12-23

Thiol separation (Å)

3

Half-sphere exposure sum ?

55

Minimum pK_a ?

10

% buried

45

Peptide accession

Residue number A

618

Residue number B

626

Peptide name

Filamin-C

Ligandability

Cysteine 618 of Filamin-C

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 626 of Filamin-C

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Filamin-C between cysteines 1906 and 1914 (58 and 66 respectively in this structure).

Details

Redox score ?

68

PDB code

Structure name

solution structure of the 17th filamin domain from human filamin c

Structure deposition date

2005-11-24

Thiol separation (Å)

5

Half-sphere exposure sum ?

51

Minimum pK_a ?

9

% buried

9

Peptide accession

Residue number A

1906

Residue number B

1914

Peptide name

Filamin-C

Ligandability

Cysteine 1906 of Filamin-C

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 1914 of Filamin-C

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-C between cysteines 2552 and 2555 (2532 and 2535 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

Structure name

crystal structure of ig-like domain 23 from human filamin c

Structure deposition date

2006-10-31

Thiol separation (Å)

9

Half-sphere exposure sum ?

35

Minimum pK_a ?

9

% buried

14

Peptide accession

Residue number A

2552

Residue number B

2555

Peptide name

Filamin-C

Ligandability

Cysteine 2552 of Filamin-C

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 2555 of Filamin-C

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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