ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Delta-1-pyrroline-5-carboxylate synthase

Intramolecular
Cysteine 584 and cysteine 612 L
Cysteine 612 and cysteine 718 L
Cysteine 584 and cysteine 718
A redox-regulated disulphide may form within Delta-1-pyrroline-5-carboxylate synthase between cysteines 584 and 612. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
60
PDB code
2h5g
Structure name
crystal structure of human pyrroline-5-carboxylate synthetase
Structure deposition date
2006-05-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
91
Minimum pKa ?
4
% buried
100
Peptide accession
P54886
Residue number A
584
Residue number B
612
Peptide name
Delta-1-pyrroline-5-carboxylate synthase

Ligandability

Cysteine 584 of Delta-1-pyrroline-5-carboxylate synthase

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 612 of Delta-1-pyrroline-5-carboxylate synthase

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 Delta-1-pyrroline-5-carboxylate synthase between cysteines 612 and 718. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
2h5g
Structure name
crystal structure of human pyrroline-5-carboxylate synthetase
Structure deposition date
2006-05-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
9
% buried
86
Peptide accession
P54886
Residue number A
612
Residue number B
718
Peptide name
Delta-1-pyrroline-5-carboxylate synthase

Ligandability

Cysteine 612 of Delta-1-pyrroline-5-carboxylate synthase

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 718 of Delta-1-pyrroline-5-carboxylate synthase

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 Delta-1-pyrroline-5-carboxylate synthase between cysteines 584 and 718. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
2h5g
Structure name
crystal structure of human pyrroline-5-carboxylate synthetase
Structure deposition date
2006-05-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
11
% buried
86
Peptide accession
P54886
Residue number A
584
Residue number B
718
Peptide name
Delta-1-pyrroline-5-carboxylate synthase

Ligandability

Cysteine 584 of Delta-1-pyrroline-5-carboxylate synthase

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 718 of Delta-1-pyrroline-5-carboxylate synthase

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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