ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7

Intermolecular
Cysteine 47 and cysteine 47
Intramolecular
Cysteine 52 and cysteine 261
Cysteine 24 and cysteine 261
A redox-regulated disulphide may form between two units of Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7 at cysteines 47 and 47.

Details

Redox score ?
82
PDB code
5nfo
Structure name
human jmjd7 in complex with mn and 2og in the p21212 form
Structure deposition date
2017-03-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide A name
Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7
Peptide B name
Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7
Peptide A accession
P0C870
Peptide B accession
P0C870
Peptide A residue number
47
Peptide B residue number
47

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.

A redox-regulated disulphide may form within Bifunctional peptidase and (3S)-lysyl hydroxylase Jmjd7 between cysteines 52 and 261. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
4qsz
Structure name
crystal structure of mouse jmjd7 fused with maltose-binding protein
Structure deposition date
2014-07-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
92
Peptide accession
P0C872
Residue number A
52
Residue number B
261
Peptide name
Bifunctional peptidase and (3S)-lysyl hydroxylase Jmjd7

Ligandability

Cysteine 52 of Bifunctional peptidase and (3S)-lysyl hydroxylase Jmjd7

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 261 of Bifunctional peptidase and (3S)-lysyl hydroxylase Jmjd7

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 Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7 between cysteines 24 and 261 (260 and 261 respectively in this structure).

Details

Redox score ?
nan
PDB code
5nfo
Structure name
human jmjd7 in complex with mn and 2og in the p21212 form
Structure deposition date
2017-03-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
68
Peptide accession
P0C870
Residue number A
24
Residue number B
261
Peptide name
Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7

Ligandability

Cysteine 24 of Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7

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 261 of Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7

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.

Uncertain whether structure cysteine 260 has been assigned to correct residue.
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