Adenosine deaminase

Intramolecular

A redox-regulated disulphide may form within Adenosine deaminase between cysteines 154 and 169. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

3iar

Structure name

the crystal structure of human adenosine deaminase

Structure deposition date

2009-07-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide accession

P00813

Residue number A

154

Residue number B

169

Peptide name

Adenosine deaminase

Ligandability

Cysteine 154 of Adenosine deaminase

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 169 of Adenosine deaminase

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 Adenosine deaminase between cysteines 153 and 154. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7rtg

Structure name

crystal structure of the human adenosine deaminase 1

Structure deposition date

2021-08-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide accession

P00813

Residue number A

153

Residue number B

154

Peptide name

Adenosine deaminase

Ligandability

Cysteine 153 of Adenosine deaminase

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 154 of Adenosine deaminase

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 Adenosine deaminase between cysteines 153 and 169. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?