ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Protein-cysteine N-palmitoyltransferase HHAT

Intramolecular
Cysteine 105 and cysteine 107
Cysteine 126 and cysteine 139
Cysteine 139 and cysteine 177
A redox-regulated disulphide may form within Protein-cysteine N-palmitoyltransferase HHAT between cysteines 105 and 107. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7mhy
Structure name
human hedgehog acyltransferase (hhat) in complex with palmitoyl-coa and two fab antibody fragments
Structure deposition date
2021-04-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
11
% buried
66
Peptide accession
Q5VTY9
Residue number A
105
Residue number B
107
Peptide name
Protein-cysteine N-palmitoyltransferase HHAT

Ligandability

Cysteine 105 of Protein-cysteine N-palmitoyltransferase HHAT

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 107 of Protein-cysteine N-palmitoyltransferase HHAT

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 Protein-cysteine N-palmitoyltransferase HHAT between cysteines 126 and 139. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
7urf
Structure name
human hhat h379c in complex with shh n-terminal peptide
Structure deposition date
2022-04-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
22
Peptide accession
Q5VTY9
Residue number A
126
Residue number B
139
Peptide name
Protein-cysteine N-palmitoyltransferase HHAT

Ligandability

Cysteine 126 of Protein-cysteine N-palmitoyltransferase HHAT

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 139 of Protein-cysteine N-palmitoyltransferase HHAT

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 Protein-cysteine N-palmitoyltransferase HHAT between cysteines 139 and 177. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
7mhz
Structure name
human hedgehog acyltransferase (hhat) in complex with a palmitoylated hedgehog peptide product and a fab antibody fragment
Structure deposition date
2021-04-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
74
Peptide accession
Q5VTY9
Residue number A
139
Residue number B
177
Peptide name
Protein-cysteine N-palmitoyltransferase HHAT

Ligandability

Cysteine 139 of Protein-cysteine N-palmitoyltransferase HHAT

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 177 of Protein-cysteine N-palmitoyltransferase HHAT

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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