Myocardial zonula adherens protein

Intramolecular

A redox-regulated disulphide may form within Myocardial zonula adherens protein between cysteines 362 and 124 (102 and 124 respectively in this structure).

Details

Redox score ?

nan

PDB code

2kxs

Structure name

zo1 zu5 domain in complex with grinl1a peptide

Structure deposition date

2010-05-12

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

D2E9U7

Residue number A

362

Residue number B

124

Peptide name

Myocardial zonula adherens protein

Ligandability

Cysteine 362 of Myocardial zonula adherens protein

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 124 of Myocardial zonula adherens protein

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.

Uncertain whether structure cysteine 102 has been assigned to correct residue.

Cysteine 124 in protein B could not be asigned to a Uniprot residue.

A redox-regulated disulphide may form within Myocardial zonula adherens protein between cysteines 362 and 111 (102 and 111 respectively in this structure).