ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Lipoyltransferase 1, mitochondrial

Intramolecular
Cysteine 182 and cysteine 224
Cysteine 310 and cysteine 324
Cysteine 324 and cysteine 366
A redox-regulated disulphide may form within Lipoyltransferase 1, mitochondrial between cysteines 182 and 224 (156 and 198 respectively in this structure).

Details

Redox score ?
73
PDB code
2e5a
Structure name
crystal structure of bovine lipoyltransferase in complex with lipoyl-amp
Structure deposition date
2006-12-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
8
% buried
81
Peptide accession
O46419
Residue number A
182
Residue number B
224
Peptide name
Lipoyltransferase 1, mitochondrial

Ligandability

Cysteine 182 of Lipoyltransferase 1, 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 224 of Lipoyltransferase 1, 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 Lipoyltransferase 1, mitochondrial between cysteines 310 and 324 (284 and 298 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3a7u
Structure name
crystal structure of the bovine lipoyltransferase in its unliganded form
Structure deposition date
2009-10-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
58
Peptide accession
O46419
Residue number A
310
Residue number B
324
Peptide name
Lipoyltransferase 1, mitochondrial

Ligandability

Cysteine 310 of Lipoyltransferase 1, 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 324 of Lipoyltransferase 1, 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 Lipoyltransferase 1, mitochondrial between cysteines 324 and 366 (298 and 340 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
3a7u
Structure name
crystal structure of the bovine lipoyltransferase in its unliganded form
Structure deposition date
2009-10-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
11
% buried
60
Peptide accession
O46419
Residue number A
324
Residue number B
366
Peptide name
Lipoyltransferase 1, mitochondrial

Ligandability

Cysteine 324 of Lipoyltransferase 1, 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 366 of Lipoyltransferase 1, 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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