ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Cytochrome P450 11B2, mitochondrial

Intramolecular
Cysteine 109 and cysteine 152
Cysteine 450 and cysteine 109
Cysteine 450 and cysteine 112
A redox-regulated disulphide may form within Cytochrome P450 11B2, mitochondrial between cysteines 109 and 152 (115 and 152 respectively in this structure).

Details

Redox score ?
nan
PDB code
7m8i
Structure name
human cyp11b2 and human adrenodoxin in complex with fadrozole
Structure deposition date
2021-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
8
% buried
92
Peptide accession
P19099
Residue number A
109
Residue number B
152
Peptide name
Cytochrome P450 11B2, mitochondrial

Ligandability

Cysteine 109 of Cytochrome P450 11B2, 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 152 of Cytochrome P450 11B2, 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 152 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Cytochrome P450 11B2, mitochondrial between cysteines 450 and 109 (106 and 115 respectively in this structure).

Details

Redox score ?
nan
PDB code
7m8i
Structure name
human cyp11b2 and human adrenodoxin in complex with fadrozole
Structure deposition date
2021-03-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
77
Minimum pKa ?
6
% buried
98
Peptide accession
P19099
Residue number A
450
Residue number B
109
Peptide name
Cytochrome P450 11B2, mitochondrial

Ligandability

Cysteine 450 of Cytochrome P450 11B2, 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 109 of Cytochrome P450 11B2, 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.

Uncertain whether structure cysteine 106 has been assigned to correct residue.
A redox-regulated disulphide may form within Cytochrome P450 11B2, mitochondrial between cysteines 450 and 112 (106 and 112 respectively in this structure).

Details

Redox score ?
nan
PDB code
7m8i
Structure name
human cyp11b2 and human adrenodoxin in complex with fadrozole
Structure deposition date
2021-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
5
% buried
84
Peptide accession
P19099
Residue number A
450
Residue number B
112
Peptide name
Cytochrome P450 11B2, mitochondrial

Ligandability

Cysteine 450 of Cytochrome P450 11B2, 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 112 of Cytochrome P450 11B2, 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.

Uncertain whether structure cysteine 106 has been assigned to correct residue.
Cysteine 112 in protein B could not be asigned to a Uniprot residue.
If this tool was useful for finding a disulphide, please cite: