ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Cytochrome c

Intermolecular
Cysteine 18 and cysteine 18
Cysteine 18 and cysteine 124 of Cytochrome c1, heme protein, mitochondrial
Intramolecular
Cysteine 15 and cysteine 18
A redox-regulated disulphide may form between two units of Cytochrome c at cysteines 18 and 18 (17 and 17 respectively in this structure).

Details

Redox score ?
62
PDB code
6ecj
Structure name
human cytochrome c g41t
Structure deposition date
2018-08-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
100
Peptide A name
Cytochrome c
Peptide B name
Cytochrome c
Peptide A accession
P99999
Peptide B accession
P99999
Peptide A residue number
18
Peptide B residue number
18

Ligandability

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 18 of Cytochrome c and cysteine 124 of Cytochrome c1, heme protein, mitochondrial (17 and 40 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
2ybb
Structure name
fitted model for bovine mitochondrial supercomplex i1iii2iv1 by single particle cryo-em (emd-1876)
Structure deposition date
2011-03-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
13
% buried
97
Peptide A name
Cytochrome c
Peptide B name
Cytochrome c1, heme protein, mitochondrial
Peptide A accession
P62894
Peptide B accession
P00125
Peptide A residue number
18
Peptide B residue number
124

Ligandability

Cysteine 18 of Cytochrome c

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 124 of Cytochrome c1, heme protein, 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 Cytochrome c between cysteines 15 and 18 (14 and 17 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
5exq
Structure name
human cytochrome c y48h
Structure deposition date
2015-11-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
13
% buried
92
Peptide accession
P99999
Residue number A
15
Residue number B
18
Peptide name
Cytochrome c

Ligandability

Cysteine 15 of Cytochrome c

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 18 of Cytochrome c

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.

If this tool was useful for finding a disulphide, please cite: