ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Selenocysteine lyase

Intramolecular
Cysteine 101 and cysteine 177
Cysteine 129 and cysteine 390
Cysteine 375 and cysteine 601
A redox-regulated disulphide may form within Selenocysteine lyase between cysteines 101 and 177. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3a9z
Structure name
crystal structure of ras selenocysteine lyase in complex with selenopropionate
Structure deposition date
2009-11-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
58
Peptide accession
Q68FT9
Residue number A
101
Residue number B
177
Peptide name
Selenocysteine lyase

Ligandability

Cysteine 101 of Selenocysteine lyase

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 177 of Selenocysteine lyase

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 Selenocysteine lyase between cysteines 129 and 390. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3a9z
Structure name
crystal structure of ras selenocysteine lyase in complex with selenopropionate
Structure deposition date
2009-11-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
92
Peptide accession
Q68FT9
Residue number A
129
Residue number B
390
Peptide name
Selenocysteine lyase

Ligandability

Cysteine 129 of Selenocysteine lyase

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 390 of Selenocysteine lyase

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 Selenocysteine lyase between cysteines 375 and 601.

Details

Redox score ?
nan
PDB code
3a9y
Structure name
crystal structure of rat selenocysteine lyase in complex with l- cysteine
Structure deposition date
2009-11-09
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
13
% buried
nan
Peptide accession
Q68FT9
Residue number A
375
Residue number B
601
Peptide name
Selenocysteine lyase

Ligandability

Cysteine 375 of Selenocysteine lyase

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 601 of Selenocysteine lyase

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 601 in protein B could not be asigned to a Uniprot residue.
If this tool was useful for finding a disulphide, please cite: