ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Hypermethylated in cancer 2 protein

Intramolecular
Cysteine 563 and cysteine 566
Cysteine 507 and cysteine 510
Cysteine 535 and cysteine 538
A redox-regulated disulphide may form within Hypermethylated in cancer 2 protein between cysteines 563 and 566.

Details

Redox score ?
90
PDB code
7txc
Structure name
hic2 zinc finger domain in complex with the dna binding motif-2 of the bcl11a enhancer
Structure deposition date
2022-02-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
5
% buried
0
Peptide accession
Q96JB3
Residue number A
563
Residue number B
566
Peptide name
Hypermethylated in cancer 2 protein

Ligandability

Cysteine 563 of Hypermethylated in cancer 2 protein

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 566 of Hypermethylated in cancer 2 protein

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 Hypermethylated in cancer 2 protein between cysteines 507 and 510.

Details

Redox score ?
88
PDB code
7txc
Structure name
hic2 zinc finger domain in complex with the dna binding motif-2 of the bcl11a enhancer
Structure deposition date
2022-02-08
Thiol separation (Å)
3
Half-sphere exposure sum ?
38
Minimum pKa ?
7
% buried
0
Peptide accession
Q96JB3
Residue number A
507
Residue number B
510
Peptide name
Hypermethylated in cancer 2 protein

Ligandability

Cysteine 507 of Hypermethylated in cancer 2 protein

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 510 of Hypermethylated in cancer 2 protein

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 Hypermethylated in cancer 2 protein between cysteines 535 and 538.

Details

Redox score ?
84
PDB code
7txc
Structure name
hic2 zinc finger domain in complex with the dna binding motif-2 of the bcl11a enhancer
Structure deposition date
2022-02-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
7
% buried
0
Peptide accession
Q96JB3
Residue number A
535
Residue number B
538
Peptide name
Hypermethylated in cancer 2 protein

Ligandability

Cysteine 535 of Hypermethylated in cancer 2 protein

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 538 of Hypermethylated in cancer 2 protein

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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