ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Mammalian ependymin-related protein 1

Intramolecular
Cysteine 88 and cysteine 222
Cysteine 113 and cysteine 210
Cysteine 42 and cysteine 172
A redox-regulated disulphide may form within Mammalian ependymin-related protein 1 between cysteines 88 and 222.

Details

Redox score ?
89
PDB code
6e8n
Structure name
crystal structure of glycosylated human epdr1
Structure deposition date
2018-07-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UM22
Residue number A
88
Residue number B
222
Peptide name
Mammalian ependymin-related protein 1

Ligandability

Cysteine 88 of Mammalian ependymin-related protein 1

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 222 of Mammalian ependymin-related protein 1

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 Mammalian ependymin-related protein 1 between cysteines 113 and 210.

Details

Redox score ?
88
PDB code
6jld
Structure name
crystal structure of a human ependymin related protein
Structure deposition date
2019-03-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UM22
Residue number A
113
Residue number B
210
Peptide name
Mammalian ependymin-related protein 1

Ligandability

Cysteine 113 of Mammalian ependymin-related protein 1

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 210 of Mammalian ependymin-related protein 1

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 Mammalian ependymin-related protein 1 between cysteines 42 and 172.

Details

Redox score ?
82
PDB code
6jld
Structure name
crystal structure of a human ependymin related protein
Structure deposition date
2019-03-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UM22
Residue number A
42
Residue number B
172
Peptide name
Mammalian ependymin-related protein 1

Ligandability

Cysteine 42 of Mammalian ependymin-related protein 1

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 172 of Mammalian ependymin-related protein 1

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.

If this tool was useful for finding a disulphide, please cite: