ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Aconitate hydratase, mitochondrial

Intramolecular
Cysteine 448 and cysteine 451 L
Cysteine 385 and cysteine 451 L
Cysteine 385 and cysteine 448 L
Cysteine 205 and cysteine 284
Cysteine 277 and cysteine 284
A redox-regulated disulphide may form within Aconitate hydratase, mitochondrial between cysteines 448 and 451 (421 and 424 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
5acn
Structure name
structure of activated aconitase
Structure deposition date
1990-01-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
94
Minimum pKa ?
12
% buried
100
Peptide accession
P16276
Residue number A
448
Residue number B
451
Peptide name
Aconitate hydratase, mitochondrial

Ligandability

Cysteine 448 of Aconitate hydratase, 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 451 of Aconitate hydratase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

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 Aconitate hydratase, mitochondrial between cysteines 385 and 451 (358 and 424 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
1fgh
Structure name
complex with 4-hydroxy-trans-aconitate
Structure deposition date
1996-09-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
96
Minimum pKa ?
12
% buried
100
Peptide accession
P20004
Residue number A
385
Residue number B
451
Peptide name
Aconitate hydratase, mitochondrial

Ligandability

Cysteine 385 of Aconitate hydratase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

Ligandable in the dataset of Vinogradova et al.

Ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 451 of Aconitate hydratase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

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 Aconitate hydratase, mitochondrial between cysteines 385 and 448 (358 and 421 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
1ami
Structure name
steric and conformational features of the aconitase mechanism
Structure deposition date
1994-11-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
99
Minimum pKa ?
14
% buried
100
Peptide accession
P20004
Residue number A
385
Residue number B
448
Peptide name
Aconitate hydratase, mitochondrial

Ligandability

Cysteine 385 of Aconitate hydratase, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

Ligandable in the dataset of Vinogradova et al.

Ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 448 of Aconitate hydratase, 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 Aconitate hydratase, mitochondrial between cysteines 205 and 284 (178 and 257 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
1b0k
Structure name
s642a:fluorocitrate complex of aconitase
Structure deposition date
1998-11-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
101
Minimum pKa ?
12
% buried
100
Peptide accession
P16276
Residue number A
205
Residue number B
284
Peptide name
Aconitate hydratase, mitochondrial

Ligandability

Cysteine 205 of Aconitate hydratase, 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 284 of Aconitate hydratase, 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 Aconitate hydratase, mitochondrial between cysteines 277 and 284 (250 and 257 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
1c97
Structure name
s642a:isocitrate complex of aconitase
Structure deposition date
1999-07-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
99
Minimum pKa ?
13
% buried
100
Peptide accession
P20004
Residue number A
277
Residue number B
284
Peptide name
Aconitate hydratase, mitochondrial

Ligandability

Cysteine 277 of Aconitate hydratase, 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 284 of Aconitate hydratase, 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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