Aspartyl aminopeptidase

A redox-regulated disulphide may form within Aspartyl aminopeptidase between cysteines 48 and 279 (38 and 269 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4dyo

Structure name

crystal structure of human aspartyl aminopeptidase (dnpep) in complex with aspartic acid hydroxamate

Structure deposition date

2012-02-29

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide accession

Q9ULA0

Residue number A

Residue number B

279

Peptide name

Aspartyl aminopeptidase

Ligandability

Cysteine 48 of Aspartyl aminopeptidase

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 279 of Aspartyl aminopeptidase

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 Aspartyl aminopeptidase between cysteines 267 and 443. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7u5h

Structure name

cryo-em structure of dnpep

Structure deposition date

2022-03-02

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide accession

Q2HJH1

Residue number A

267

Residue number B

443

Peptide name

Aspartyl aminopeptidase

Ligandability

Cysteine 267 of Aspartyl aminopeptidase

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 443 of Aspartyl aminopeptidase

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 Aspartyl aminopeptidase between cysteines 265 and 267 (290 and 292 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?