a tool for identifying drug-targetable redox-active disulphides

V-type proton ATPase catalytic subunit A

Intermolecular

Cysteine 138 and cysteine 32 of Purine NTPase L

A redox-regulated disulphide may form between cysteine 138 of V-type proton ATPase catalytic subunit A and cysteine 32 of Purine NTPase. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

39

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 ?

62

Minimum pK_a ?

10

% buried

81

Peptide A name

V-type proton ATPase catalytic subunit A

Peptide B name

Purine NTPase

Peptide A accession

Peptide B accession

Peptide A residue number

138

Peptide B residue number

32

Ligandability

Cysteine 138 of V-type proton ATPase catalytic subunit A

Ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

Ligandable in the dataset of Vinogradova et al.

Ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 32 of Purine NTPase

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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