ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Vesicle-fusing ATPase

Intramolecular
Cysteine 11 and cysteine 21
Cysteine 568 and cysteine 582 L
Cysteine 568 and cysteine 599
A redox-regulated disulphide may form within Vesicle-fusing ATPase between cysteines 11 and 21. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
1qcs
Structure name
n-terminal domain of n-ethylmaleimide sensitive factor (nsf)
Structure deposition date
1999-05-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
64
Peptide accession
P18708
Residue number A
11
Residue number B
21
Peptide name
Vesicle-fusing ATPase

Ligandability

Cysteine 11 of Vesicle-fusing ATPase

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 21 of Vesicle-fusing ATPase

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 Vesicle-fusing ATPase between cysteines 568 and 582. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
6mdp
Structure name
the d1 and d2 domain rings of nsf engaging the snap-25 n-terminus within the 20s supercomplex (focused refinement on d1/d2 rings, class 2)
Structure deposition date
2018-09-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
80
Peptide accession
P18708
Residue number A
568
Residue number B
582
Peptide name
Vesicle-fusing ATPase

Ligandability

Cysteine 568 of Vesicle-fusing ATPase

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 582 of Vesicle-fusing ATPase

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.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Vesicle-fusing ATPase between cysteines 568 and 599. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
3j94
Structure name
structure of atp-bound n-ethylmaleimide sensitive factor determined by single particle cryoelectron microscopy
Structure deposition date
2014-12-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
100
Peptide accession
P18708
Residue number A
568
Residue number B
599
Peptide name
Vesicle-fusing ATPase

Ligandability

Cysteine 568 of Vesicle-fusing ATPase

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 599 of Vesicle-fusing ATPase

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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