ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Dopamine beta-hydroxylase

Intermolecular
Cysteine 528 and cysteine 530
Cysteine 528 and cysteine 528
Cysteine 154 and cysteine 154
Cysteine 154 and cysteine 596
Cysteine 530 and cysteine 530
A redox-regulated disulphide may form between two units of Dopamine beta-hydroxylase at cysteines 528 and 530.

Details

Redox score ?
87
PDB code
4zel
Structure name
human dopamine beta-hydroxylase
Structure deposition date
2015-04-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
32
Minimum pKa ?
nan
% buried
nan
Peptide A name
Dopamine beta-hydroxylase
Peptide B name
Dopamine beta-hydroxylase
Peptide A accession
P09172
Peptide B accession
P09172
Peptide A residue number
528
Peptide B residue number
530

Ligandability

Cysteine 528 of Dopamine beta-hydroxylase

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 530 of Dopamine beta-hydroxylase

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 two units of Dopamine beta-hydroxylase at cysteines 528 and 528.

Details

Redox score ?
73
PDB code
4zel
Structure name
human dopamine beta-hydroxylase
Structure deposition date
2015-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide A name
Dopamine beta-hydroxylase
Peptide B name
Dopamine beta-hydroxylase
Peptide A accession
P09172
Peptide B accession
P09172
Peptide A residue number
528
Peptide B residue number
528

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 two units of Dopamine beta-hydroxylase at cysteines 154 and 154. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
4zel
Structure name
human dopamine beta-hydroxylase
Structure deposition date
2015-04-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
nan
Peptide A name
Dopamine beta-hydroxylase
Peptide B name
Dopamine beta-hydroxylase
Peptide A accession
P09172
Peptide B accession
P09172
Peptide A residue number
154
Peptide B residue number
154

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 two units of Dopamine beta-hydroxylase at cysteines 154 and 596. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
4zel
Structure name
human dopamine beta-hydroxylase
Structure deposition date
2015-04-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
nan
Peptide A name
Dopamine beta-hydroxylase
Peptide B name
Dopamine beta-hydroxylase
Peptide A accession
P09172
Peptide B accession
P09172
Peptide A residue number
154
Peptide B residue number
596

Ligandability

Cysteine 154 of Dopamine beta-hydroxylase

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 596 of Dopamine beta-hydroxylase

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 two units of Dopamine beta-hydroxylase at cysteines 530 and 530. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
4zel
Structure name
human dopamine beta-hydroxylase
Structure deposition date
2015-04-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
34
Minimum pKa ?
nan
% buried
nan
Peptide A name
Dopamine beta-hydroxylase
Peptide B name
Dopamine beta-hydroxylase
Peptide A accession
P09172
Peptide B accession
P09172
Peptide A residue number
530
Peptide B residue number
530

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.

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