ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Endoribonuclease ZC3H12A

Intramolecular
Cysteine 306 and cysteine 318
Cysteine 312 and cysteine 318
Cysteine 306 and cysteine 312
A redox-regulated disulphide may form within Endoribonuclease ZC3H12A between cysteines 306 and 318.

Details

Redox score ?
90
PDB code
2n5k
Structure name
regnase-1 zinc finger domain
Structure deposition date
2015-07-18
Thiol separation (Å)
3
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
0
Peptide accession
Q5D1E7
Residue number A
306
Residue number B
318
Peptide name
Endoribonuclease ZC3H12A

Ligandability

Cysteine 306 of Endoribonuclease ZC3H12A

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 318 of Endoribonuclease ZC3H12A

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 Endoribonuclease ZC3H12A between cysteines 312 and 318.

Details

Redox score ?
88
PDB code
2n5k
Structure name
regnase-1 zinc finger domain
Structure deposition date
2015-07-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
7
% buried
0
Peptide accession
Q5D1E7
Residue number A
312
Residue number B
318
Peptide name
Endoribonuclease ZC3H12A

Ligandability

Cysteine 312 of Endoribonuclease ZC3H12A

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 318 of Endoribonuclease ZC3H12A

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 Endoribonuclease ZC3H12A between cysteines 306 and 312.

Details

Redox score ?
84
PDB code
2n5k
Structure name
regnase-1 zinc finger domain
Structure deposition date
2015-07-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
7
% buried
0
Peptide accession
Q5D1E7
Residue number A
306
Residue number B
312
Peptide name
Endoribonuclease ZC3H12A

Ligandability

Cysteine 306 of Endoribonuclease ZC3H12A

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 312 of Endoribonuclease ZC3H12A

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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