ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Palmitoyltransferase ZDHHC20

Intermolecular
Cysteine 263 and cysteine 263 L
Intramolecular
Cysteine 145 and cysteine 162
Cysteine 128 and cysteine 131
Cysteine 142 and cysteine 162
Cysteine 128 and cysteine 148
Cysteine 142 and cysteine 145
Cysteine 131 and cysteine 148
Cysteine 131 and cysteine 142
Cysteine 142 and cysteine 148
Cysteine 232 and cysteine 263 L
Cysteine 156 and cysteine 162
A redox-regulated disulphide may form between two units of Palmitoyltransferase ZDHHC20 at cysteines 263 and 263.

Details

Redox score ?
72
PDB code
6bmm
Structure name
structure of human dhhc20 palmitoyltransferase, space group p21
Structure deposition date
2017-11-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
43
Peptide A name
Palmitoyltransferase ZDHHC20
Peptide B name
Palmitoyltransferase ZDHHC20
Peptide A accession
Q5W0Z9
Peptide B accession
Q5W0Z9
Peptide A residue number
263
Peptide B residue number
263

Ligandability

A redox-regulated disulphide may form within Palmitoyltransferase ZDHHC20 between cysteines 145 and 162.

Details

Redox score ?
94
PDB code
6bmm
Structure name
structure of human dhhc20 palmitoyltransferase, space group p21
Structure deposition date
2017-11-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
66
Minimum pKa ?
3
% buried
52
Peptide accession
Q5W0Z9
Residue number A
145
Residue number B
162
Peptide name
Palmitoyltransferase ZDHHC20

Ligandability

Cysteine 145 of Palmitoyltransferase ZDHHC20

Cysteine 162 of Palmitoyltransferase ZDHHC20

A redox-regulated disulphide may form within Palmitoyltransferase ZDHHC20 between cysteines 128 and 131.

Details

Redox score ?
86
PDB code
6bmn
Structure name
structure of human dhhc20 palmitoyltransferase, space group p63
Structure deposition date
2017-11-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
53
Minimum pKa ?
7
% buried
26
Peptide accession
Q5W0Z9
Residue number A
128
Residue number B
131
Peptide name
Palmitoyltransferase ZDHHC20

Ligandability

Cysteine 128 of Palmitoyltransferase ZDHHC20

Cysteine 131 of Palmitoyltransferase ZDHHC20

A redox-regulated disulphide may form within Palmitoyltransferase ZDHHC20 between cysteines 142 and 162.

Details

Redox score ?
79
PDB code
6bmm
Structure name
structure of human dhhc20 palmitoyltransferase, space group p21
Structure deposition date
2017-11-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
65
Minimum pKa ?
9
% buried
48
Peptide accession
Q5W0Z9
Residue number A
142
Residue number B
162
Peptide name
Palmitoyltransferase ZDHHC20

Ligandability

Cysteine 142 of Palmitoyltransferase ZDHHC20

Cysteine 162 of Palmitoyltransferase ZDHHC20

A redox-regulated disulphide may form within Palmitoyltransferase ZDHHC20 between cysteines 128 and 148.

Details

Redox score ?
79
PDB code
6bmn
Structure name
structure of human dhhc20 palmitoyltransferase, space group p63
Structure deposition date
2017-11-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
7
% buried
50
Peptide accession
Q5W0Z9
Residue number A
128
Residue number B
148
Peptide name
Palmitoyltransferase ZDHHC20

Ligandability

Cysteine 128 of Palmitoyltransferase ZDHHC20

Cysteine 148 of Palmitoyltransferase ZDHHC20

A redox-regulated disulphide may form within Palmitoyltransferase ZDHHC20 between cysteines 142 and 145.

Details

Redox score ?
74
PDB code
6bml
Structure name
structure of human dhhc20 palmitoyltransferase, irreversibly inhibited by 2-bromopalmitate
Structure deposition date
2017-11-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
nan
Peptide accession
Q5W0Z9
Residue number A
142
Residue number B
145
Peptide name
Palmitoyltransferase ZDHHC20

Ligandability

Cysteine 142 of Palmitoyltransferase ZDHHC20

Cysteine 145 of Palmitoyltransferase ZDHHC20

A redox-regulated disulphide may form within Palmitoyltransferase ZDHHC20 between cysteines 131 and 148.

Details

Redox score ?
73
PDB code
6bmn
Structure name
structure of human dhhc20 palmitoyltransferase, space group p63
Structure deposition date
2017-11-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
46
Peptide accession
Q5W0Z9
Residue number A
131
Residue number B
148
Peptide name
Palmitoyltransferase ZDHHC20

Ligandability

Cysteine 131 of Palmitoyltransferase ZDHHC20

Cysteine 148 of Palmitoyltransferase ZDHHC20

A redox-regulated disulphide may form within Palmitoyltransferase ZDHHC20 between cysteines 131 and 142. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
6bmm
Structure name
structure of human dhhc20 palmitoyltransferase, space group p21
Structure deposition date
2017-11-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
20
Peptide accession
Q5W0Z9
Residue number A
131
Residue number B
142
Peptide name
Palmitoyltransferase ZDHHC20

Ligandability

Cysteine 131 of Palmitoyltransferase ZDHHC20

Cysteine 142 of Palmitoyltransferase ZDHHC20

A redox-regulated disulphide may form within Palmitoyltransferase ZDHHC20 between cysteines 142 and 148. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
7khm
Structure name
crystal structure of hdhhs20 bound to palmitoyl coa
Structure deposition date
2020-10-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
7
% buried
42
Peptide accession
Q5W0Z9
Residue number A
142
Residue number B
148
Peptide name
Palmitoyltransferase ZDHHC20

Ligandability

Cysteine 142 of Palmitoyltransferase ZDHHC20

Cysteine 148 of Palmitoyltransferase ZDHHC20

A redox-regulated disulphide may form within Palmitoyltransferase ZDHHC20 between cysteines 232 and 263. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6bmm
Structure name
structure of human dhhc20 palmitoyltransferase, space group p21
Structure deposition date
2017-11-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
11
% buried
46
Peptide accession
Q5W0Z9
Residue number A
232
Residue number B
263
Peptide name
Palmitoyltransferase ZDHHC20

Ligandability

Cysteine 232 of Palmitoyltransferase ZDHHC20

Cysteine 263 of Palmitoyltransferase ZDHHC20

A redox-regulated disulphide may form within Palmitoyltransferase ZDHHC20 between cysteines 156 and 162. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
6bml
Structure name
structure of human dhhc20 palmitoyltransferase, irreversibly inhibited by 2-bromopalmitate
Structure deposition date
2017-11-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
14
% buried
76
Peptide accession
Q5W0Z9
Residue number A
156
Residue number B
162
Peptide name
Palmitoyltransferase ZDHHC20

Ligandability

Cysteine 156 of Palmitoyltransferase ZDHHC20

Cysteine 162 of Palmitoyltransferase ZDHHC20

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