ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

6-phosphogluconate dehydrogenase, decarboxylating

Intramolecular
Cysteine 170 and cysteine 366 L
Cysteine 170 and cysteine 171 L
Cysteine 199 and cysteine 422
A redox-regulated disulphide may form within 6-phosphogluconate dehydrogenase, decarboxylating between cysteines 170 and 366 (169 and 365 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
1pgq
Structure name
crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for nadp specificity and the enzyme mechanism
Structure deposition date
1994-07-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
84
Minimum pKa ?
11
% buried
84
Peptide accession
P00349
Residue number A
170
Residue number B
366
Peptide name
6-phosphogluconate dehydrogenase, decarboxylating

Ligandability

Cysteine 170 of 6-phosphogluconate dehydrogenase, decarboxylating

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 366 of 6-phosphogluconate dehydrogenase, decarboxylating

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 6-phosphogluconate dehydrogenase, decarboxylating between cysteines 170 and 171. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
2jkv
Structure name
structure of human phosphogluconate dehydrogenase in complex with nadph at 2
Structure deposition date
2008-09-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
11
% buried
84
Peptide accession
P52209
Residue number A
170
Residue number B
171
Peptide name
6-phosphogluconate dehydrogenase, decarboxylating

Ligandability

Cysteine 170 of 6-phosphogluconate dehydrogenase, decarboxylating

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 171 of 6-phosphogluconate dehydrogenase, decarboxylating

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 6-phosphogluconate dehydrogenase, decarboxylating between cysteines 199 and 422 (198 and 421 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
1pgq
Structure name
crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for nadp specificity and the enzyme mechanism
Structure deposition date
1994-07-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
88
Peptide accession
P00349
Residue number A
199
Residue number B
422
Peptide name
6-phosphogluconate dehydrogenase, decarboxylating

Ligandability

Cysteine 199 of 6-phosphogluconate dehydrogenase, decarboxylating

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 422 of 6-phosphogluconate dehydrogenase, decarboxylating

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: