Triple functional domain protein

Intramolecular

Cysteine 2062 and cysteine 2142

A redox-regulated disulphide may form within Triple functional domain protein between cysteines 1442 and 1443 (1383 and 1384 respectively in this structure).

Details

Redox score ?

PDB code

1nty

Structure name

crystal structure of the first dh/ph domain of trio to 1

Structure deposition date

2003-01-30

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

O75962

Residue number A

1442

Residue number B

1443

Peptide name

Triple functional domain protein

Ligandability

Cysteine 1442 of Triple functional domain 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 1443 of Triple functional domain 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.

A redox-regulated disulphide may form within Triple functional domain protein between cysteines 2062 and 2142.

Details

Redox score ?

PDB code

6d8z

Structure name

crystal structure of the c-terminal guanine nucleotide exchange factor module of human trio

Structure deposition date

2018-04-27

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

O75962

Residue number A

2062

Residue number B

2142

Peptide name

Triple functional domain protein

Ligandability

Cysteine 2062 of Triple functional domain 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 2142 of Triple functional domain 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.

A redox-regulated disulphide may form within Triple functional domain protein between cysteines 2222 and 2224. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?