TMEM106B protein

Intermolecular

A redox-regulated disulphide may form between two units of TMEM106B protein at cysteines 293 and 293 (253 and 253 respectively in this structure).

Details

Redox score ?

PDB code

7u18

Structure name

tmem106b(120-254) t185s protofilament from frontotemporal lobar degeneration with tdp-43 pathology (ftld-tdp) type a (all cases combined)

Structure deposition date

2022-02-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

TMEM106B protein

Peptide B name

TMEM106B protein

Peptide A accession

Q8N353

Peptide B accession

Q8N353

Peptide A residue number

293

Peptide B residue number

293

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 TMEM106B protein at cysteines 254 and 254 (214 and 214 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7u18

Structure name

tmem106b(120-254) t185s protofilament from frontotemporal lobar degeneration with tdp-43 pathology (ftld-tdp) type a (all cases combined)

Structure deposition date

2022-02-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

TMEM106B protein

Peptide B name

TMEM106B protein

Peptide A accession

Q8N353

Peptide B accession

Q8N353

Peptide A residue number

254

Peptide B residue number

254

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 TMEM106B protein at cysteines 254 and 293 (214 and 253 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?