ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Protein transport protein Sec61 subunit alpha isoform 1

Intramolecular
Cysteine 45 and cysteine 46
Cysteine 46 and cysteine 188
Cysteine 372 and cysteine 427
A redox-regulated disulphide may form within Protein transport protein Sec61 subunit alpha isoform 1 between cysteines 45 and 46. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
4cg7
Structure name
cryo-em of the sec61-complex bound to the idle 80s ribosome
Structure deposition date
2013-11-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
9
% buried
96
Peptide accession
P38377
Residue number A
45
Residue number B
46
Peptide name
Protein transport protein Sec61 subunit alpha isoform 1

Ligandability

Cysteine 45 of Protein transport protein Sec61 subunit alpha isoform 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 46 of Protein transport protein Sec61 subunit alpha isoform 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 Protein transport protein Sec61 subunit alpha isoform 1 between cysteines 46 and 188. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
3jc2
Structure name
the structure of the mammalian sec61 channel opened by a signal sequence
Structure deposition date
2015-11-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
58
Peptide accession
P38377
Residue number A
46
Residue number B
188
Peptide name
Protein transport protein Sec61 subunit alpha isoform 1

Ligandability

Cysteine 46 of Protein transport protein Sec61 subunit alpha isoform 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 188 of Protein transport protein Sec61 subunit alpha isoform 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 Protein transport protein Sec61 subunit alpha isoform 1 between cysteines 372 and 427 (349 and 404 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
8b6l
Structure name
subtomogram average of the human sec61-trap-osta-translocon
Structure deposition date
2022-09-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
46
Peptide accession
P61619
Residue number A
372
Residue number B
427
Peptide name
Protein transport protein Sec61 subunit alpha isoform 1

Ligandability

Cysteine 372 of Protein transport protein Sec61 subunit alpha isoform 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 427 of Protein transport protein Sec61 subunit alpha isoform 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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