Sorcin

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Sorcin at cysteines 57 and 75. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2jc2

Structure name

the crystal structure of the natural f112l human sorcin mutant

Structure deposition date

2006-12-19

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Sorcin

Peptide B name

Sorcin

Peptide A accession

P30626

Peptide B accession

P30626

Peptide A residue number

Peptide B residue number

Ligandability

Cysteine 57 of Sorcin

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 75 of Sorcin

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sorcin between cysteines 162 and 163. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4usl

Structure name

the x-ray structure of calcium bound human sorcin

Structure deposition date

2014-07-10

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

P30626

Residue number A

162

Residue number B

163

Peptide name

Sorcin

Ligandability

Cysteine 162 of Sorcin

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 163 of Sorcin

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Sorcin between cysteines 57 and 75. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?