ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cysteine desulfurase

Intermolecular
Cysteine 381 and cysteine 69 of Iron-sulfur cluster assembly enzyme ISCU
Cysteine 381 and cysteine 130 of Iron-sulfur cluster assembly enzyme ISCU
Cysteine 381 and cysteine 95 of Iron-sulfur cluster assembly enzyme ISCU
Cysteine 381 and cysteine 138 of Iron-sulfur cluster assembly enzyme ISCU
Cysteine 308 and cysteine 50 of Frataxin, mitochondrial
Intramolecular
Cysteine 158 and cysteine 381 L
Cysteine 158 and cysteine 163 L
A redox-regulated disulphide may form between cysteine 381 of Cysteine desulfurase and cysteine 69 of Iron-sulfur cluster assembly enzyme ISCU (381 and 44 respectively in this structure).

Details

Redox score ?
77
PDB code
5wlw
Structure name
crystal structure of the human mitochondrial cysteine desulfurase with active cysteine loop within iscu1 active site, coordinating zn ion
Structure deposition date
2017-07-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
75
Minimum pKa ?
4
% buried
62
Peptide A name
Cysteine desulfurase
Peptide B name
Iron-sulfur cluster assembly enzyme ISCU
Peptide A accession
Q9Y697
Peptide B accession
Q9H1K1
Peptide A residue number
381
Peptide B residue number
69

Ligandability

Cysteine 381 of Cysteine desulfurase

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 69 of Iron-sulfur cluster assembly enzyme ISCU

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 between cysteine 381 of Cysteine desulfurase and cysteine 130 of Iron-sulfur cluster assembly enzyme ISCU. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
5kz5
Structure name
architecture of the human mitochondrial iron-sulfur cluster assembly machinery: the complex formed by the iron donor, the sulfur donor, and the scaffold
Structure deposition date
2016-07-22
Thiol separation (Å)
6
Half-sphere exposure sum ?
83
Minimum pKa ?
10
% buried
100
Peptide A name
Cysteine desulfurase
Peptide B name
Iron-sulfur cluster assembly enzyme ISCU
Peptide A accession
Q9Y697
Peptide B accession
Q9H1K1
Peptide A residue number
381
Peptide B residue number
130

Ligandability

Cysteine 381 of Cysteine desulfurase

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 130 of Iron-sulfur cluster assembly enzyme ISCU

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 between cysteine 381 of Cysteine desulfurase and cysteine 95 of Iron-sulfur cluster assembly enzyme ISCU (381 and 70 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
5wlw
Structure name
crystal structure of the human mitochondrial cysteine desulfurase with active cysteine loop within iscu1 active site, coordinating zn ion
Structure deposition date
2017-07-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
91
Minimum pKa ?
14
% buried
86
Peptide A name
Cysteine desulfurase
Peptide B name
Iron-sulfur cluster assembly enzyme ISCU
Peptide A accession
Q9Y697
Peptide B accession
Q9H1K1
Peptide A residue number
381
Peptide B residue number
95

Ligandability

Cysteine 381 of Cysteine desulfurase

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 95 of Iron-sulfur cluster assembly enzyme ISCU

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 between cysteine 381 of Cysteine desulfurase and cysteine 138 of Iron-sulfur cluster assembly enzyme ISCU (381 and 113 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5wlw
Structure name
crystal structure of the human mitochondrial cysteine desulfurase with active cysteine loop within iscu1 active site, coordinating zn ion
Structure deposition date
2017-07-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
87
Minimum pKa ?
16
% buried
80
Peptide A name
Cysteine desulfurase
Peptide B name
Iron-sulfur cluster assembly enzyme ISCU
Peptide A accession
Q9Y697
Peptide B accession
Q9H1K1
Peptide A residue number
381
Peptide B residue number
138

Ligandability

Cysteine 381 of Cysteine desulfurase

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 138 of Iron-sulfur cluster assembly enzyme ISCU

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 between cysteine 308 of Cysteine desulfurase and cysteine 50 of Frataxin, mitochondrial. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
5kz5
Structure name
architecture of the human mitochondrial iron-sulfur cluster assembly machinery: the complex formed by the iron donor, the sulfur donor, and the scaffold
Structure deposition date
2016-07-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
11
% buried
92
Peptide A name
Cysteine desulfurase
Peptide B name
Frataxin, mitochondrial
Peptide A accession
Q9Y697
Peptide B accession
Q16595
Peptide A residue number
308
Peptide B residue number
50

Ligandability

Cysteine 308 of Cysteine desulfurase

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 50 of Frataxin, 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 Cysteine desulfurase between cysteines 158 and 381. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
6w1d
Structure name
structure of human mitochondrial complex nfs1-iscu2 (wt)-isd11 with e
Structure deposition date
2020-03-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
85
Peptide accession
Q9Y697
Residue number A
158
Residue number B
381
Peptide name
Cysteine desulfurase

Ligandability

Cysteine 158 of Cysteine desulfurase

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 381 of Cysteine desulfurase

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 Cysteine desulfurase between cysteines 158 and 163. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
5usr
Structure name
crystal structure of human nfs1-isd11 in complex with e
Structure deposition date
2017-02-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
70
Peptide accession
Q9Y697
Residue number A
158
Residue number B
163
Peptide name
Cysteine desulfurase

Ligandability

Cysteine 158 of Cysteine desulfurase

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 163 of Cysteine desulfurase

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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