ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Endoplasmic reticulum resident protein 44

Intermolecular
Cysteine 245 of Peroxiredoxin-4 and cysteine 58 L
Intramolecular
Cysteine 189 and cysteine 241
Cysteine 301 and cysteine 318
Cysteine 58 and cysteine 92
A redox-regulated disulphide may form between cysteine 245 of Peroxiredoxin-4 and cysteine 58 of Endoplasmic reticulum resident protein 44 (245 and 29 respectively in this structure).

Details

Redox score ?
82
PDB code
5hqp
Structure name
crystal structure of the erp44-peroxiredoxin 4 complex
Structure deposition date
2016-01-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide A name
Peroxiredoxin-4
Peptide B name
Endoplasmic reticulum resident protein 44
Peptide A accession
Q13162
Peptide B accession
Q9BS26
Peptide A residue number
245
Peptide B residue number
58

Ligandability

Cysteine 245 of Peroxiredoxin-4

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 58 of Endoplasmic reticulum resident protein 44

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 resident protein 44 between cysteines 189 and 241 (160 and 212 respectively in this structure).

Details

Redox score ?
74
PDB code
5hqp
Structure name
crystal structure of the erp44-peroxiredoxin 4 complex
Structure deposition date
2016-01-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
8
% buried
76
Peptide accession
Q9BS26
Residue number A
189
Residue number B
241
Peptide name
Endoplasmic reticulum resident protein 44

Ligandability

Cysteine 189 of Endoplasmic reticulum resident protein 44

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 241 of Endoplasmic reticulum resident protein 44

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 resident protein 44 between cysteines 301 and 318 (272 and 289 respectively in this structure).

Details

Redox score ?
72
PDB code
5gu6
Structure name
crystal structure of human erp44 form i
Structure deposition date
2016-08-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
40
Peptide accession
Q9BS26
Residue number A
301
Residue number B
318
Peptide name
Endoplasmic reticulum resident protein 44

Ligandability

Cysteine 301 of Endoplasmic reticulum resident protein 44

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 Endoplasmic reticulum resident protein 44

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 resident protein 44 between cysteines 58 and 92 (29 and 63 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
2r2j
Structure name
crystal structure of human erp44
Structure deposition date
2007-08-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
8
% buried
52
Peptide accession
Q9BS26
Residue number A
58
Residue number B
92
Peptide name
Endoplasmic reticulum resident protein 44

Ligandability

Cysteine 58 of Endoplasmic reticulum resident protein 44

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 92 of Endoplasmic reticulum resident protein 44

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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