ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Legumain

Intermolecular
Cysteine 189 and cysteine 189
Intramolecular
Cysteine 390 and cysteine 429
Cysteine 378 and cysteine 412
A redox-regulated disulphide may form between two units of Legumain at cysteines 189 and 189. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
4awb
Structure name
crystal structure of active legumain in complex with aan-cmk
Structure deposition date
2012-06-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
100
Minimum pKa ?
16
% buried
100
Peptide A name
Legumain
Peptide B name
Legumain
Peptide A accession
Q99538
Peptide B accession
Q99538
Peptide A residue number
189
Peptide B residue number
189

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 within Legumain between cysteines 390 and 429.

Details

Redox score ?
85
PDB code
4fgu
Structure name
crystal structure of prolegumain
Structure deposition date
2012-06-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99538
Residue number A
390
Residue number B
429
Peptide name
Legumain

Ligandability

Cysteine 390 of Legumain

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 429 of Legumain

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 Legumain between cysteines 378 and 412.

Details

Redox score ?
82
PDB code
4fgu
Structure name
crystal structure of prolegumain
Structure deposition date
2012-06-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99538
Residue number A
378
Residue number B
412
Peptide name
Legumain

Ligandability

Cysteine 378 of Legumain

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 412 of Legumain

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: