ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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von Hippel-Lindau disease tumor suppressor

Intermolecular
Cysteine 542 of Endothelial PAS domain-containing protein 1 and cysteine 77 L
Cysteine 112 of Elongin-C and cysteine 162
Cysteine 77 and cysteine 77 L
A redox-regulated disulphide may form between cysteine 542 of Endothelial PAS domain-containing protein 1 and cysteine 77 of von Hippel-Lindau disease tumor suppressor.

Details

Redox score ?
86
PDB code
6i7q
Structure name
structure of pvhl-elongin b-elongin c (vcb) in complex with hydroxylated-hif-2alpha (523-542) in the c2221 form
Structure deposition date
2018-11-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
Endothelial PAS domain-containing protein 1
Peptide B name
von Hippel-Lindau disease tumor suppressor
Peptide A accession
Q99814
Peptide B accession
P40337
Peptide A residue number
542
Peptide B residue number
77

Ligandability

Cysteine 542 of Endothelial PAS domain-containing protein 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 77 of von Hippel-Lindau disease tumor suppressor

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 542 in protein A could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form between cysteine 112 of Elongin-C and cysteine 162 of von Hippel-Lindau disease tumor suppressor. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6i7q
Structure name
structure of pvhl-elongin b-elongin c (vcb) in complex with hydroxylated-hif-2alpha (523-542) in the c2221 form
Structure deposition date
2018-11-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
13
% buried
96
Peptide A name
Elongin-C
Peptide B name
von Hippel-Lindau disease tumor suppressor
Peptide A accession
Q2KII4
Peptide B accession
P40337
Peptide A residue number
112
Peptide B residue number
162

Ligandability

Cysteine 112 of Elongin-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 162 of von Hippel-Lindau disease tumor suppressor

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 between two units of von Hippel-Lindau disease tumor suppressor at cysteines 77 and 77. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
6sis
Structure name
crystal structure of macrocyclic protac 1 in complex with the second bromodomain of human brd4 and pvhl:elonginc:elonginb
Structure deposition date
2019-08-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
100
Peptide A name
von Hippel-Lindau disease tumor suppressor
Peptide B name
von Hippel-Lindau disease tumor suppressor
Peptide A accession
P40337
Peptide B accession
P40337
Peptide A residue number
77
Peptide B residue number
77

Ligandability

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.

Ligandable in the dataset of Kuljanin et al.

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