DCN1-like protein 1

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of DCN1-like protein 1 at cysteines 115 and 115. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5ufi

Structure name

dcn1 bound to di-591

Structure deposition date

2017-01-04

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

DCN1-like protein 1

Peptide B name

DCN1-like protein 1

Peptide A accession

Q96GG9

Peptide B accession

Q96GG9

Peptide A residue number

115

Peptide B residue number

115

Ligandability

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.

A redox-regulated disulphide may form within DCN1-like protein 1 between cysteines 90 and 115. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

3tdu

Structure name

n-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex: structure of a human cul1whb- dcn1p-acetylated ubc12n complex

Structure deposition date

2011-08-11

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q96GG9

Residue number A

Residue number B

115

Peptide name