ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Serine palmitoyltransferase 1

Intermolecular
Cysteine 133 and cysteine 511 of Serine palmitoyltransferase 2 L
Intramolecular
Cysteine 318 and cysteine 319
Cysteine 100 and cysteine 419
A redox-regulated disulphide may form between cysteine 133 of Serine palmitoyltransferase 1 and cysteine 511 of Serine palmitoyltransferase 2. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
6m4n
Structure name
cryo-em structure of the dimeric spt-ormdl3 complex
Structure deposition date
2020-03-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
98
Minimum pKa ?
10
% buried
100
Peptide A name
Serine palmitoyltransferase 1
Peptide B name
Serine palmitoyltransferase 2
Peptide A accession
O15269
Peptide B accession
O15270
Peptide A residue number
133
Peptide B residue number
511

Ligandability

Cysteine 133 of Serine palmitoyltransferase 1

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.

Ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 511 of Serine palmitoyltransferase 2

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 Serine palmitoyltransferase 1 between cysteines 318 and 319. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7cqi
Structure name
cryo-em structure of the substrate-bound spt-ormdl3 complex
Structure deposition date
2020-08-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
94
Minimum pKa ?
12
% buried
100
Peptide accession
O15269
Residue number A
318
Residue number B
319
Peptide name
Serine palmitoyltransferase 1

Ligandability

Cysteine 318 of Serine palmitoyltransferase 1

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 319 of Serine palmitoyltransferase 1

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 Serine palmitoyltransferase 1 between cysteines 100 and 419. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
7k0n
Structure name
human serine palmitoyltransferase complex sptlc1/spltc2/ssspta/ormdl3, class 2
Structure deposition date
2020-09-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
58
Peptide accession
O15269
Residue number A
100
Residue number B
419
Peptide name
Serine palmitoyltransferase 1

Ligandability

Cysteine 100 of Serine palmitoyltransferase 1

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 419 of Serine palmitoyltransferase 1

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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