ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial

Intramolecular
Cysteine 164 and cysteine 192
Cysteine 304 and cysteine 357
Cysteine 198 and cysteine 373 L
Cysteine 281 and cysteine 304
Cysteine 281 and cysteine 319
Cysteine 281 and cysteine 357
A redox-regulated disulphide may form within Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial between cysteines 164 and 192.

Details

Redox score ?
70
PDB code
2aex
Structure name
the 1
Structure deposition date
2005-07-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
8
% buried
76
Peptide accession
P36551
Residue number A
164
Residue number B
192
Peptide name
Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial

Ligandability

Cysteine 164 of Oxygen-dependent coproporphyrinogen-III oxidase, 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 192 of Oxygen-dependent coproporphyrinogen-III oxidase, 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 Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial between cysteines 304 and 357.

Details

Redox score ?
67
PDB code
2aex
Structure name
the 1
Structure deposition date
2005-07-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
9
% buried
94
Peptide accession
P36551
Residue number A
304
Residue number B
357
Peptide name
Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial

Ligandability

Cysteine 304 of Oxygen-dependent coproporphyrinogen-III oxidase, 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 357 of Oxygen-dependent coproporphyrinogen-III oxidase, 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 Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial between cysteines 198 and 373. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
2aex
Structure name
the 1
Structure deposition date
2005-07-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
9
Peptide accession
P36551
Residue number A
198
Residue number B
373
Peptide name
Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial

Ligandability

Cysteine 198 of Oxygen-dependent coproporphyrinogen-III oxidase, 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 373 of Oxygen-dependent coproporphyrinogen-III oxidase, 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 Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial between cysteines 281 and 304. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
2aex
Structure name
the 1
Structure deposition date
2005-07-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
9
% buried
94
Peptide accession
P36551
Residue number A
281
Residue number B
304
Peptide name
Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial

Ligandability

Cysteine 281 of Oxygen-dependent coproporphyrinogen-III oxidase, 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 304 of Oxygen-dependent coproporphyrinogen-III oxidase, 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 Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial between cysteines 281 and 319. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
2aex
Structure name
the 1
Structure deposition date
2005-07-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
13
% buried
100
Peptide accession
P36551
Residue number A
281
Residue number B
319
Peptide name
Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial

Ligandability

Cysteine 281 of Oxygen-dependent coproporphyrinogen-III oxidase, 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 319 of Oxygen-dependent coproporphyrinogen-III oxidase, 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 Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial between cysteines 281 and 357. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
2aex
Structure name
the 1
Structure deposition date
2005-07-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
91
Minimum pKa ?
13
% buried
100
Peptide accession
P36551
Residue number A
281
Residue number B
357
Peptide name
Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial

Ligandability

Cysteine 281 of Oxygen-dependent coproporphyrinogen-III oxidase, 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 357 of Oxygen-dependent coproporphyrinogen-III oxidase, 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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