ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Pyruvate kinase

Intermolecular
Cysteine 352 and cysteine 66
Intramolecular
Cysteine 458 and cysteine 459
Cysteine 393 and cysteine 501
A redox-regulated disulphide may form between two units of Pyruvate kinase at cysteines 352 and 66 (329 and 43 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
5scj
Structure name
structure of liver pyruvate kinase in complex with anthraquinone derivative 106
Structure deposition date
2021-12-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
92
Peptide A name
Pyruvate kinase
Peptide B name
Pyruvate kinase
Peptide A accession
Q16716
Peptide B accession
Q16716
Peptide A residue number
352
Peptide B residue number
66

Ligandability

Cysteine 352 of Pyruvate kinase

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 66 of Pyruvate kinase

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 Pyruvate kinase between cysteines 458 and 459 (435 and 436 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5sdt
Structure name
structure of liver pyruvate kinase in complex with anthraquinone derivative 15
Structure deposition date
2022-01-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
100
Peptide accession
Q16716
Residue number A
458
Residue number B
459
Peptide name
Pyruvate kinase

Ligandability

Cysteine 458 of Pyruvate kinase

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 459 of Pyruvate kinase

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 Pyruvate kinase between cysteines 393 and 501 (370 and 478 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
5sck
Structure name
structure of liver pyruvate kinase in complex with anthraquinone derivative 42
Structure deposition date
2021-12-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
96
Minimum pKa ?
12
% buried
100
Peptide accession
Q16716
Residue number A
393
Residue number B
501
Peptide name
Pyruvate kinase

Ligandability

Cysteine 393 of Pyruvate kinase

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 501 of Pyruvate kinase

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: