ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Protein ERGIC-53

Intermolecular
Cysteine 198 and cysteine 198 L
Intramolecular
Cysteine 198 and cysteine 238 L
A redox-regulated disulphide may form between two units of Protein ERGIC-53 at cysteines 198 and 198. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
1r1z
Structure name
the crystal structure of the carbohydrate recognition domain of the glycoprotein sorting receptor p58/ergic-53 reveals a novel metal binding site and conformational changes associated with calcium ion binding
Structure deposition date
2003-09-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide A name
Protein ERGIC-53
Peptide B name
Protein ERGIC-53
Peptide A accession
Q62902
Peptide B accession
Q62902
Peptide A residue number
198
Peptide B residue number
198

Ligandability

Not ligandable in the dataset of Yang et al.

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 Protein ERGIC-53 between cysteines 198 and 238.

Details

Redox score ?
80
PDB code
1r1z
Structure name
the crystal structure of the carbohydrate recognition domain of the glycoprotein sorting receptor p58/ergic-53 reveals a novel metal binding site and conformational changes associated with calcium ion binding
Structure deposition date
2003-09-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q62902
Residue number A
198
Residue number B
238
Peptide name
Protein ERGIC-53

Ligandability

Cysteine 198 of Protein ERGIC-53

Not ligandable in the dataset of Yang et al.

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 238 of Protein ERGIC-53

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.

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