a tool for identifying drug-targetable redox-active disulphides

V-type proton ATPase 21 kDa proteolipid subunit c''

Intramolecular

Cysteine 18 and cysteine 25

Cysteine 151 and cysteine 154

Cysteine 97 and cysteine 151

Cysteine 97 and cysteine 154

A redox-regulated disulphide may form within V-type proton ATPase 21 kDa proteolipid subunit c'' between cysteines 18 and 25. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

44

PDB code

Structure name

human v-atpase in state 2 with sidk and adp

Structure deposition date

2020-04-20

Thiol separation (Å)

9

Half-sphere exposure sum ?

33

Minimum pK_a ?

9

% buried

12

Peptide accession

Residue number A

18

Residue number B

25

Peptide name

V-type proton ATPase 21 kDa proteolipid subunit c''

Ligandability

Cysteine 18 of V-type proton ATPase 21 kDa proteolipid subunit c''

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 25 of V-type proton ATPase 21 kDa proteolipid subunit c''

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 21 kDa proteolipid subunit c'' between cysteines 151 and 154. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

41

PDB code

Structure name

human v-atpase in state 3 with sidk and adp

Structure deposition date

2020-04-20

Thiol separation (Å)

6

Half-sphere exposure sum ?

107

Minimum pK_a ?

12

% buried

100

Peptide accession

Residue number A

151

Residue number B

154

Peptide name

V-type proton ATPase 21 kDa proteolipid subunit c''

Ligandability

Cysteine 151 of V-type proton ATPase 21 kDa proteolipid subunit c''

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 154 of V-type proton ATPase 21 kDa proteolipid subunit c''

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 21 kDa proteolipid subunit c'' between cysteines 97 and 151. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

33

PDB code

Structure name

human v-atpase in state 3 with sidk and adp

Structure deposition date

2020-04-20

Thiol separation (Å)

8

Half-sphere exposure sum ?

109

Minimum pK_a ?

12

% buried

100

Peptide accession

Residue number A

97

Residue number B

151

Peptide name

V-type proton ATPase 21 kDa proteolipid subunit c''

Ligandability

Cysteine 97 of V-type proton ATPase 21 kDa proteolipid subunit c''

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 151 of V-type proton ATPase 21 kDa proteolipid subunit c''

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 21 kDa proteolipid subunit c'' between cysteines 97 and 154. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

25

PDB code

Structure name

the vo region of human v-atpase in state 1 (focused refinement)

Structure deposition date

2020-04-20

Thiol separation (Å)

10

Half-sphere exposure sum ?

99

Minimum pK_a ?

11

% buried

100

Peptide accession

Residue number A

97

Residue number B

154

Peptide name

V-type proton ATPase 21 kDa proteolipid subunit c''

Ligandability

Cysteine 97 of V-type proton ATPase 21 kDa proteolipid subunit c''

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 154 of V-type proton ATPase 21 kDa proteolipid subunit c''

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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