ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Gamma-butyrobetaine dioxygenase

Intramolecular
Cysteine 40 and cysteine 43
Cysteine 38 and cysteine 40
Cysteine 38 and cysteine 43
A redox-regulated disulphide may form within Gamma-butyrobetaine dioxygenase between cysteines 40 and 43.

Details

Redox score ?
79
PDB code
4c8r
Structure name
human gamma-butyrobetaine dioxygenase (bbox1) in complex with ni(ii) and n-(3-hydroxypicolinoyl)-s-(pyridin-2-ylmethyl)-l-cysteine (ar692b)
Structure deposition date
2013-10-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
34
Peptide accession
O75936
Residue number A
40
Residue number B
43
Peptide name
Gamma-butyrobetaine dioxygenase

Ligandability

Cysteine 40 of Gamma-butyrobetaine dioxygenase

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 43 of Gamma-butyrobetaine dioxygenase

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 Gamma-butyrobetaine dioxygenase between cysteines 38 and 40.

Details

Redox score ?
77
PDB code
4c8r
Structure name
human gamma-butyrobetaine dioxygenase (bbox1) in complex with ni(ii) and n-(3-hydroxypicolinoyl)-s-(pyridin-2-ylmethyl)-l-cysteine (ar692b)
Structure deposition date
2013-10-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
8
% buried
44
Peptide accession
O75936
Residue number A
38
Residue number B
40
Peptide name
Gamma-butyrobetaine dioxygenase

Ligandability

Cysteine 38 of Gamma-butyrobetaine dioxygenase

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 40 of Gamma-butyrobetaine dioxygenase

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 Gamma-butyrobetaine dioxygenase between cysteines 38 and 43.

Details

Redox score ?
75
PDB code
4bhi
Structure name
three dimensional structure of human gamma-butyrobetaine hydroxylase in complex with 3-(1,1,1,2-tetramethylhydrazin-1-ium-2-yl)propanoate
Structure deposition date
2013-04-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
42
Peptide accession
O75936
Residue number A
38
Residue number B
43
Peptide name
Gamma-butyrobetaine dioxygenase

Ligandability

Cysteine 38 of Gamma-butyrobetaine dioxygenase

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 43 of Gamma-butyrobetaine dioxygenase

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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