ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

V-type proton ATPase subunit e 1

Intramolecular
Cysteine 44 and cysteine 48
Cysteine 44 and cysteine 47
Cysteine 47 and cysteine 48
A redox-regulated disulphide may form within V-type proton ATPase subunit e 1 between cysteines 44 and 48.

Details

Redox score ?
69
PDB code
6wm2
Structure name
human v-atpase in state 1 with sidk and adp
Structure deposition date
2020-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
91
Peptide accession
O15342
Residue number A
44
Residue number B
48
Peptide name
V-type proton ATPase subunit e 1

Ligandability

Cysteine 44 of V-type proton ATPase subunit e 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 48 of V-type proton ATPase subunit e 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 V-type proton ATPase subunit e 1 between cysteines 44 and 47. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
6wlw
Structure name
the vo region of human v-atpase in state 1 (focused refinement)
Structure deposition date
2020-04-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
94
Peptide accession
O15342
Residue number A
44
Residue number B
47
Peptide name
V-type proton ATPase subunit e 1

Ligandability

Cysteine 44 of V-type proton ATPase subunit e 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 47 of V-type proton ATPase subunit e 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 V-type proton ATPase subunit e 1 between cysteines 47 and 48. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6wlw
Structure name
the vo region of human v-atpase in state 1 (focused refinement)
Structure deposition date
2020-04-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
13
% buried
99
Peptide accession
O15342
Residue number A
47
Residue number B
48
Peptide name
V-type proton ATPase subunit e 1

Ligandability

Cysteine 47 of V-type proton ATPase subunit e 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 48 of V-type proton ATPase subunit e 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.

If this tool was useful for finding a disulphide, please cite: