ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Endoplasmic reticulum aminopeptidase 2

Intramolecular
Cysteine 503 and cysteine 514
Cysteine 421 and cysteine 460
Cysteine 759 and cysteine 766
A redox-regulated disulphide may form within Endoplasmic reticulum aminopeptidase 2 between cysteines 503 and 514.

Details

Redox score ?
80
PDB code
7nup
Structure name
endoplasmic reticulum aminopeptidase 2 complexed with a mixed hydroxamic and sulfonyl ligand
Structure deposition date
2021-03-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6P179
Residue number A
503
Residue number B
514
Peptide name
Endoplasmic reticulum aminopeptidase 2

Ligandability

Cysteine 503 of Endoplasmic reticulum aminopeptidase 2

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 514 of Endoplasmic reticulum aminopeptidase 2

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 Endoplasmic reticulum aminopeptidase 2 between cysteines 421 and 460.

Details

Redox score ?
79
PDB code
7sh0
Structure name
crystal structure of endoplasmic reticulum aminopeptidase 2 (erap2) complex with a highly selective and potent small molecule
Structure deposition date
2021-10-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6P179
Residue number A
421
Residue number B
460
Peptide name
Endoplasmic reticulum aminopeptidase 2

Ligandability

Cysteine 421 of Endoplasmic reticulum aminopeptidase 2

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 460 of Endoplasmic reticulum aminopeptidase 2

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 Endoplasmic reticulum aminopeptidase 2 between cysteines 759 and 766.

Details

Redox score ?
71
PDB code
7nsk
Structure name
endoplasmic reticulum aminopeptidase 2 complexed with a hydroxamic ligand
Structure deposition date
2021-03-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
28
Peptide accession
Q6P179
Residue number A
759
Residue number B
766
Peptide name
Endoplasmic reticulum aminopeptidase 2

Ligandability

Cysteine 759 of Endoplasmic reticulum aminopeptidase 2

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 766 of Endoplasmic reticulum aminopeptidase 2

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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