ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Epididymis luminal protein 214

Intermolecular
Cysteine 243 and cysteine 236 of Ig-like domain-containing protein
Intramolecular
Cysteine 167 and cysteine 223
Cysteine 41 and cysteine 115
Cysteine 102 and cysteine 167
A redox-regulated disulphide may form between cysteine 243 of Epididymis luminal protein 214 and cysteine 236 of Ig-like domain-containing protein (216 and 214 respectively in this structure).

Details

Redox score ?
94
PDB code
6mxr
Structure name
crystal structure of the dimeric bh1-fab variant [hc-y33w,hc-d98m,hc- g99m]
Structure deposition date
2018-10-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
Epididymis luminal protein 214
Peptide B name
Ig-like domain-containing protein
Peptide A accession
V9HW68
Peptide B accession
Q7Z3Y4
Peptide A residue number
243
Peptide B residue number
236

Ligandability

Cysteine 243 of Epididymis luminal protein 214

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 236 of Ig-like domain-containing protein

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 Epididymis luminal protein 214 between cysteines 167 and 223 (140 and 196 respectively in this structure).

Details

Redox score ?
80
PDB code
6my5
Structure name
crystal structure of the dimeric bh1-fab variant [hc-y33w,hc-d98f,hc- g99m,lc-s30br]
Structure deposition date
2018-11-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
V9HW68
Residue number A
167
Residue number B
223
Peptide name
Epididymis luminal protein 214

Ligandability

Cysteine 167 of Epididymis luminal protein 214

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 223 of Epididymis luminal protein 214

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 Epididymis luminal protein 214 between cysteines 41 and 115 (22 and 92 respectively in this structure).

Details

Redox score ?
79
PDB code
6my4
Structure name
crystal structure of the dimeric bh1-fab variant [hc-y33w,hc-d98m,hc- g99m,lc-s30br]
Structure deposition date
2018-11-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
V9HW68
Residue number A
41
Residue number B
115
Peptide name
Epididymis luminal protein 214

Ligandability

Cysteine 41 of Epididymis luminal protein 214

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 115 of Epididymis luminal protein 214

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 Epididymis luminal protein 214 between cysteines 102 and 167 (102 and 112 respectively in this structure).

Details

Redox score ?
nan
PDB code
7d03
Structure name
s protein of sars-cov-2 in complex bound with fabp5a-2g7
Structure deposition date
2020-09-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
V9HW68
Residue number A
102
Residue number B
167
Peptide name
Epididymis luminal protein 214

Ligandability

Cysteine 102 of Epididymis luminal protein 214

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 167 of Epididymis luminal protein 214

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 102 in protein A could not be asigned to a Uniprot residue.
Uncertain whether structure cysteine 112 has been assigned to correct residue.
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