ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

V-type proton ATPase subunit H

Intramolecular
Cysteine 200 and cysteine 204
Cysteine 204 and cysteine 73 L
Cysteine 47 and cysteine 186 L
Cysteine 73 and cysteine 298 L
A redox-regulated disulphide may form within V-type proton ATPase subunit H between cysteines 200 and 204 (182 and 186 respectively in this structure).

Details

Redox score ?
61
PDB code
6xbw
Structure name
cryo-em structure of v-atpase from bovine brain, state 1
Structure deposition date
2020-06-07
Thiol separation (Å)
5
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
54
Peptide accession
F1MZL6
Residue number A
200
Residue number B
204
Peptide name
V-type proton ATPase subunit H

Ligandability

Cysteine 200 of V-type proton ATPase subunit H

Cysteine 204 of V-type proton ATPase subunit H

A redox-regulated disulphide may form within V-type proton ATPase subunit H between cysteines 204 and 73 (290 and 297 respectively in this structure).

Details

Redox score ?
nan
PDB code
7fdc
Structure name
cryoem structures of reconstituted v-atpase, state3
Structure deposition date
2021-07-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
100
Peptide accession
Q9UI12
Residue number A
204
Residue number B
73
Peptide name
V-type proton ATPase subunit H

Ligandability

Cysteine 204 of V-type proton ATPase subunit H

Cysteine 73 of V-type proton ATPase subunit H

Uncertain whether structure cysteine 290 has been assigned to correct residue.
Uncertain whether structure cysteine 297 has been assigned to correct residue.
A redox-regulated disulphide may form within V-type proton ATPase subunit H between cysteines 47 and 186 (183 and 186 respectively in this structure).

Details

Redox score ?
nan
PDB code
7fda
Structure name
cryoem structure of reconstituted v-atpase, state1
Structure deposition date
2021-07-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
66
Peptide accession
Q9UI12
Residue number A
47
Residue number B
186
Peptide name
V-type proton ATPase subunit H

Ligandability

Cysteine 47 of V-type proton ATPase subunit H

Cysteine 186 of V-type proton ATPase subunit H

Uncertain whether structure cysteine 183 has been assigned to correct residue.
Cysteine 186 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within V-type proton ATPase subunit H between cysteines 73 and 298 (297 and 298 respectively in this structure).

Details

Redox score ?
nan
PDB code
7fdb
Structure name
cryoem structures of reconstituted v-atpase,state2
Structure deposition date
2021-07-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
81
Peptide accession
Q9UI12
Residue number A
73
Residue number B
298
Peptide name
V-type proton ATPase subunit H

Ligandability

Cysteine 73 of V-type proton ATPase subunit H

Cysteine 298 of V-type proton ATPase subunit H

Uncertain whether structure cysteine 297 has been assigned to correct residue.
Cysteine 298 in protein B could not be asigned to a Uniprot residue.
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