BLM protein

Intermolecular

A redox-regulated disulphide may form between two units of BLM protein at cysteines 380 and 380. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5lup

Structure name

structures of dhbn domain of human blm helicase

Structure deposition date

2016-09-09

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

BLM protein

Peptide B name

BLM protein

Peptide A accession

Q3B7X0

Peptide B accession

Q3B7X0

Peptide A residue number

380

Peptide B residue number

380

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.

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