ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Peptide deformylase, mitochondrial

Intramolecular
Cysteine 132 and cysteine 135
Cysteine 108 and cysteine 172 L
Cysteine 172 and cysteine 222
A redox-regulated disulphide may form within Peptide deformylase, mitochondrial between cysteines 132 and 135 (74 and 77 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
3g5k
Structure name
structure and activity of human mitochondrial peptide deformylase, a novel cancer target
Structure deposition date
2009-02-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
44
Minimum pKa ?
10
% buried
22
Peptide accession
Q9HBH1
Residue number A
132
Residue number B
135
Peptide name
Peptide deformylase, mitochondrial

Ligandability

Cysteine 132 of Peptide deformylase, mitochondrial

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 135 of Peptide deformylase, mitochondrial

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 Peptide deformylase, mitochondrial between cysteines 108 and 172 (50 and 114 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3g5k
Structure name
structure and activity of human mitochondrial peptide deformylase, a novel cancer target
Structure deposition date
2009-02-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
8
% buried
94
Peptide accession
Q9HBH1
Residue number A
108
Residue number B
172
Peptide name
Peptide deformylase, mitochondrial

Ligandability

Cysteine 108 of Peptide deformylase, mitochondrial

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 172 of Peptide deformylase, mitochondrial

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 Peptide deformylase, mitochondrial between cysteines 172 and 222 (114 and 164 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
3g5p
Structure name
structure and activity of human mitochondrial peptide deformylase, a novel cancer target
Structure deposition date
2009-02-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
78
Peptide accession
Q9HBH1
Residue number A
172
Residue number B
222
Peptide name
Peptide deformylase, mitochondrial

Ligandability

Cysteine 172 of Peptide deformylase, mitochondrial

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 222 of Peptide deformylase, mitochondrial

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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