a tool for identifying drug-targetable redox-active disulphides

Protein fem-1 homolog B

Intermolecular

Cysteine 186 and cysteine 608 of Folliculin-interacting protein 1

Cysteine 186 and cysteine 610 of Folliculin-interacting protein 1

Cysteine 186 and cysteine 613 of Folliculin-interacting protein 1

Intramolecular

Cysteine 129 and cysteine 157

A redox-regulated disulphide may form between cysteine 186 of Protein fem-1 homolog B and cysteine 608 of Folliculin-interacting protein 1 (186 and 580 respectively in this structure).

Details

Redox score ?

81

PDB code

Structure name

the structure of the fem1b:fnip1 complex

Structure deposition date

2021-08-02

Thiol separation (Å)

5

Half-sphere exposure sum ?

62

Minimum pK_a ?

2

% buried

nan

Peptide A name

Protein fem-1 homolog B

Peptide B name

Folliculin-interacting protein 1

Peptide A accession

Peptide B accession

Peptide A residue number

186

Peptide B residue number

608

Ligandability

Cysteine 186 of Protein fem-1 homolog 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 608 of Folliculin-interacting protein 1

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 cysteine 186 of Protein fem-1 homolog B and cysteine 610 of Folliculin-interacting protein 1 (186 and 582 respectively in this structure).

Details

Redox score ?

76

PDB code

Structure name

the structure of the fem1b:fnip1 complex

Structure deposition date

2021-08-02

Thiol separation (Å)

4

Half-sphere exposure sum ?

69

Minimum pK_a ?

7

% buried

nan

Peptide A name

Protein fem-1 homolog B

Peptide B name

Folliculin-interacting protein 1

Peptide A accession

Peptide B accession

Peptide A residue number

186

Peptide B residue number

610

Ligandability

Cysteine 186 of Protein fem-1 homolog 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 610 of Folliculin-interacting protein 1

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 cysteine 186 of Protein fem-1 homolog B and cysteine 613 of Folliculin-interacting protein 1 (186 and 585 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

51

PDB code

Structure name

the structure of the fem1b:fnip1 complex

Structure deposition date

2021-08-02

Thiol separation (Å)

4

Half-sphere exposure sum ?

56

Minimum pK_a ?

22

% buried

nan

Peptide A name

Protein fem-1 homolog B

Peptide B name

Folliculin-interacting protein 1

Peptide A accession

Peptide B accession

Peptide A residue number

186

Peptide B residue number

613

Ligandability

Cysteine 186 of Protein fem-1 homolog 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 613 of Folliculin-interacting protein 1

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 Protein fem-1 homolog B between cysteines 129 and 157.

Details

Redox score ?

65

PDB code

Structure name

crystal structure of fem1b

Structure deposition date

2019-11-14

Thiol separation (Å)

4

Half-sphere exposure sum ?

102

Minimum pK_a ?

8

% buried

100

Peptide accession

Residue number A

129

Residue number B

157

Peptide name

Protein fem-1 homolog B

Ligandability

Cysteine 129 of Protein fem-1 homolog 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 157 of Protein fem-1 homolog 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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