ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Pyruvate kinase PKM

Intermolecular
Cysteine 317 and cysteine 31
Intramolecular
Cysteine 423 and cysteine 424 L
Cysteine 317 and cysteine 326 L
Cysteine 326 and cysteine 358 L
Cysteine 358 and cysteine 474 L
A redox-regulated disulphide may form between two units of Pyruvate kinase PKM at cysteines 317 and 31. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
6v75
Structure name
crystal structure of human pkm2 in complex with l-aspartate
Structure deposition date
2019-12-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
78
Peptide A name
Pyruvate kinase PKM
Peptide B name
Pyruvate kinase PKM
Peptide A accession
P14618
Peptide B accession
P14618
Peptide A residue number
317
Peptide B residue number
31

Ligandability

Cysteine 317 of Pyruvate kinase PKM

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 31 of Pyruvate kinase PKM

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 PKM between cysteines 423 and 424. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6gg5
Structure name
crystal structure of m2 pyk in complex with tryptophan
Structure deposition date
2018-05-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
46
Peptide accession
P14618
Residue number A
423
Residue number B
424
Peptide name
Pyruvate kinase PKM

Ligandability

Cysteine 423 of Pyruvate kinase PKM

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

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 424 of Pyruvate kinase PKM

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 PKM between cysteines 317 and 326. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
4fxj
Structure name
structure of m2 pyruvate kinase in complex with phenylalanine
Structure deposition date
2012-07-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
100
Peptide accession
P14618
Residue number A
317
Residue number B
326
Peptide name
Pyruvate kinase PKM

Ligandability

Cysteine 317 of Pyruvate kinase PKM

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 326 of Pyruvate kinase PKM

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.

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 PKM between cysteines 326 and 358. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
23
PDB code
6gg5
Structure name
crystal structure of m2 pyk in complex with tryptophan
Structure deposition date
2018-05-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
95
Minimum pKa ?
12
% buried
100
Peptide accession
P14618
Residue number A
326
Residue number B
358
Peptide name
Pyruvate kinase PKM

Ligandability

Cysteine 326 of Pyruvate kinase PKM

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 358 of Pyruvate kinase PKM

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.

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 PKM between cysteines 358 and 474 (358 and 601 respectively in this structure).

Details

Redox score ?
nan
PDB code
6nu1
Structure name
crystal structure of human pkm2 in complex with l-cysteine
Structure deposition date
2019-01-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
12
% buried
nan
Peptide accession
P14618
Residue number A
358
Residue number B
474
Peptide name
Pyruvate kinase PKM

Ligandability

Cysteine 358 of Pyruvate kinase PKM

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 474 of Pyruvate kinase PKM

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.

Uncertain whether structure cysteine 601 has been assigned to correct residue.
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