ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Alpha-soluble NSF attachment protein

Intramolecular
Cysteine 66 and cysteine 103
Cysteine 42 and cysteine 84
Cysteine 66 and cysteine 84
A redox-regulated disulphide may form within Alpha-soluble NSF attachment protein between cysteines 66 and 103.

Details

Redox score ?
77
PDB code
6mdm
Structure name
the 20s supercomplex engaging the snap-25 n-terminus (class 1)
Structure deposition date
2018-09-04
Thiol separation (Å)
3
Half-sphere exposure sum ?
75
Minimum pKa ?
7
% buried
58
Peptide accession
P54921
Residue number A
66
Residue number B
103
Peptide name
Alpha-soluble NSF attachment protein

Ligandability

Cysteine 66 of Alpha-soluble NSF attachment protein

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 103 of Alpha-soluble NSF attachment protein

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 Alpha-soluble NSF attachment protein between cysteines 42 and 84. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3j99
Structure name
structure of 20s supercomplex determined by single particle cryoelectron microscopy (state iiib)
Structure deposition date
2014-12-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
80
Peptide accession
P54921
Residue number A
42
Residue number B
84
Peptide name
Alpha-soluble NSF attachment protein

Ligandability

Cysteine 42 of Alpha-soluble NSF attachment protein

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 84 of Alpha-soluble NSF attachment protein

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 Alpha-soluble NSF attachment protein between cysteines 66 and 84. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6mdm
Structure name
the 20s supercomplex engaging the snap-25 n-terminus (class 1)
Structure deposition date
2018-09-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
7
% buried
70
Peptide accession
P54921
Residue number A
66
Residue number B
84
Peptide name
Alpha-soluble NSF attachment protein

Ligandability

Cysteine 66 of Alpha-soluble NSF attachment protein

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 84 of Alpha-soluble NSF attachment protein

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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