ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Pyruvate kinase PKLR

Intermolecular
Cysteine 74 and cysteine 360
Intramolecular
Cysteine 466 and cysteine 467
Cysteine 401 and cysteine 509
Cysteine 369 and cysteine 401
A redox-regulated disulphide may form between two units of Pyruvate kinase PKLR at cysteines 74 and 360 (43 and 329 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4ima
Structure name
the structure of c436m-hlpyk in complex with citrate/mn/atp/fru-1,6-bp
Structure deposition date
2013-01-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
90
Peptide A name
Pyruvate kinase PKLR
Peptide B name
Pyruvate kinase PKLR
Peptide A accession
O75758
Peptide B accession
O75758
Peptide A residue number
74
Peptide B residue number
360

Ligandability

Cysteine 74 of Pyruvate kinase PKLR

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 360 of Pyruvate kinase PKLR

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 PKLR between cysteines 466 and 467 (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 ?
43
PDB code
7qdn
Structure name
structure of human liver pyruvate kinase from which the b domain has been deleted
Structure deposition date
2021-11-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
86
Peptide accession
P30613
Residue number A
466
Residue number B
467
Peptide name
Pyruvate kinase PKLR

Ligandability

Cysteine 466 of Pyruvate kinase PKLR

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 467 of Pyruvate kinase PKLR

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 PKLR between cysteines 401 and 509 (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
4ima
Structure name
the structure of c436m-hlpyk in complex with citrate/mn/atp/fru-1,6-bp
Structure deposition date
2013-01-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
91
Minimum pKa ?
12
% buried
100
Peptide accession
O75758
Residue number A
401
Residue number B
509
Peptide name
Pyruvate kinase PKLR

Ligandability

Cysteine 401 of Pyruvate kinase PKLR

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 509 of Pyruvate kinase PKLR

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 PKLR between cysteines 369 and 401. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
22
PDB code
2vgi
Structure name
human erythrocyte pyruvate kinase: r486w mutant
Structure deposition date
2007-11-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
98
Minimum pKa ?
12
% buried
100
Peptide accession
P30613
Residue number A
369
Residue number B
401
Peptide name
Pyruvate kinase PKLR

Ligandability

Cysteine 369 of Pyruvate kinase PKLR

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 401 of Pyruvate kinase PKLR

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.

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