ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cytochrome c1, heme protein, mitochondrial

Intermolecular
Cysteine 67 of Cytochrome b-c1 complex subunit 6, mitochondrial and cysteine 219 L
Cysteine 18 of Cytochrome c and cysteine 124
Intramolecular
Cysteine 121 and cysteine 124
Cysteine 121 and cysteine 271
A redox-regulated disulphide may form between cysteine 67 of Cytochrome b-c1 complex subunit 6, mitochondrial and cysteine 219 of Cytochrome c1, heme protein, mitochondrial. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5xte
Structure name
cryo-em structure of human respiratory complex iii (cytochrome bc1 complex)
Structure deposition date
2017-06-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
11
% buried
58
Peptide A name
Cytochrome b-c1 complex subunit 6, mitochondrial
Peptide B name
Cytochrome c1, heme protein, mitochondrial
Peptide A accession
P07919
Peptide B accession
P08574
Peptide A residue number
67
Peptide B residue number
219

Ligandability

Cysteine 67 of Cytochrome b-c1 complex subunit 6, 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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 219 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 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 c1, heme protein, mitochondrial between cysteines 121 and 124 (37 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 ?
40
PDB code
1ppj
Structure name
bovine cytochrome bc1 complex with stigmatellin and antimycin
Structure deposition date
2003-06-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
74
Peptide accession
P00125
Residue number A
121
Residue number B
124
Peptide name
Cytochrome c1, heme protein, mitochondrial

Ligandability

Cysteine 121 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.

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 c1, heme protein, mitochondrial between cysteines 121 and 271 (37 and 187 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
1sqv
Structure name
crystal structure analysis of bovine bc1 with uhdbt
Structure deposition date
2004-03-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
13
% buried
100
Peptide accession
P00125
Residue number A
121
Residue number B
271
Peptide name
Cytochrome c1, heme protein, mitochondrial

Ligandability

Cysteine 121 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.

Cysteine 271 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.

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