ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Trifunctional enzyme subunit alpha, mitochondrial

Intramolecular
Cysteine 550 and cysteine 688
Cysteine 688 and cysteine 747
Cysteine 97 and cysteine 145 L
Cysteine 145 and cysteine 156 L
A redox-regulated disulphide may form within Trifunctional enzyme subunit alpha, mitochondrial between cysteines 550 and 688.

Details

Redox score ?
65
PDB code
6dv2
Structure name
crystal structure of human mitochondrial trifunctional protein
Structure deposition date
2018-06-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
100
Peptide accession
P40939
Residue number A
550
Residue number B
688
Peptide name
Trifunctional enzyme subunit alpha, mitochondrial

Ligandability

Cysteine 550 of Trifunctional enzyme subunit alpha, 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 688 of Trifunctional enzyme subunit alpha, 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 Trifunctional enzyme subunit alpha, mitochondrial between cysteines 688 and 747. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6dv2
Structure name
crystal structure of human mitochondrial trifunctional protein
Structure deposition date
2018-06-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
86
Peptide accession
P40939
Residue number A
688
Residue number B
747
Peptide name
Trifunctional enzyme subunit alpha, mitochondrial

Ligandability

Cysteine 688 of Trifunctional enzyme subunit alpha, 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 747 of Trifunctional enzyme subunit alpha, 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 Trifunctional enzyme subunit alpha, mitochondrial between cysteines 97 and 145. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6dv2
Structure name
crystal structure of human mitochondrial trifunctional protein
Structure deposition date
2018-06-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
10
% buried
78
Peptide accession
P40939
Residue number A
97
Residue number B
145
Peptide name
Trifunctional enzyme subunit alpha, mitochondrial

Ligandability

Cysteine 97 of Trifunctional enzyme subunit alpha, 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 145 of Trifunctional enzyme subunit alpha, 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.

A redox-regulated disulphide may form within Trifunctional enzyme subunit alpha, mitochondrial between cysteines 145 and 156. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6dv2
Structure name
crystal structure of human mitochondrial trifunctional protein
Structure deposition date
2018-06-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
11
% buried
100
Peptide accession
P40939
Residue number A
145
Residue number B
156
Peptide name
Trifunctional enzyme subunit alpha, mitochondrial

Ligandability

Cysteine 145 of Trifunctional enzyme subunit alpha, 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 156 of Trifunctional enzyme subunit alpha, 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.

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