ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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V-type proton ATPase subunit

Intramolecular
Cysteine 197 and cysteine 209
Cysteine 209 and cysteine 244
Cysteine 197 and cysteine 244
A redox-regulated disulphide may form within V-type proton ATPase subunit between cysteines 197 and 209. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
6vq6
Structure name
mammalian v-atpase from rat brain - composite model of rotational state 1 bound to adp and sidk (built from focused refinement models)
Structure deposition date
2020-02-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
68
Peptide accession
Q5M7T6
Residue number A
197
Residue number B
209
Peptide name
V-type proton ATPase subunit

Ligandability

Cysteine 197 of V-type proton ATPase subunit

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 209 of V-type proton ATPase subunit

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 V-type proton ATPase subunit between cysteines 209 and 244. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6vq6
Structure name
mammalian v-atpase from rat brain - composite model of rotational state 1 bound to adp and sidk (built from focused refinement models)
Structure deposition date
2020-02-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
54
Peptide accession
Q5M7T6
Residue number A
209
Residue number B
244
Peptide name
V-type proton ATPase subunit

Ligandability

Cysteine 209 of V-type proton ATPase subunit

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 244 of V-type proton ATPase subunit

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 V-type proton ATPase subunit between cysteines 197 and 244. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6vq7
Structure name
mammalian v-atpase from rat brain - composite model of rotational state 2 bound to adp and sidk (built from focused refinement models)
Structure deposition date
2020-02-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
13
% buried
68
Peptide accession
Q5M7T6
Residue number A
197
Residue number B
244
Peptide name
V-type proton ATPase subunit

Ligandability

Cysteine 197 of V-type proton ATPase subunit

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 244 of V-type proton ATPase subunit

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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