ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Bifunctional peptidase and arginyl-hydroxylase JMJD5

Intermolecular
Cysteine 232 and cysteine 232
A redox-regulated disulphide may form between two units of Bifunctional peptidase and arginyl-hydroxylase JMJD5 at cysteines 232 and 232.

Details

Redox score ?
71
PDB code
6f4n
Structure name
human jmjd5 in complex with mn and 2og
Structure deposition date
2017-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
26
Peptide A name
Bifunctional peptidase and arginyl-hydroxylase JMJD5
Peptide B name
Bifunctional peptidase and arginyl-hydroxylase JMJD5
Peptide A accession
Q8N371
Peptide B accession
Q8N371
Peptide A residue number
232
Peptide B residue number
232

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.

Not ligandable in the dataset of Kuljanin et al.

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