Isoaspartyl peptidase/L-asparaginase

Intermolecular

A redox-regulated disulphide may form between two units of Isoaspartyl peptidase/L-asparaginase at cysteines 202 and 202. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4osx

Structure name

structure of uncleaved glycine-bound human l-asparaginase protein

Structure deposition date

2014-02-13

Thiol separation (Å)

Half-sphere exposure sum ?

110

Minimum pK_a ?

% buried

100

Peptide A name

Isoaspartyl peptidase/L-asparaginase

Peptide B name

Isoaspartyl peptidase/L-asparaginase

Peptide A accession

Q7L266

Peptide B accession

Q7L266

Peptide A residue number

202

Peptide B residue number

202

Ligandability

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 between two units of Isoaspartyl peptidase/L-asparaginase at cysteines 115 and 202. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?