ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Protocadherin-15

Intermolecular
Cysteine 268 and cysteine 268
Cysteine 1392 and cysteine 35 of LHFPL tetraspan subfamily member 5 protein
Cysteine 277 and cysteine 268
Intramolecular
Cysteine 273 and cysteine 282
Cysteine 37 and cysteine 125
Cysteine 1392 and cysteine 1393
A redox-regulated disulphide may form between two units of Protocadherin-15 at cysteines 268 and 268 (247 and 247 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
6e8f
Structure name
crystal structure of human protocadherin-15 ec3-5 cd2-1
Structure deposition date
2018-07-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide A name
Protocadherin-15
Peptide B name
Protocadherin-15
Peptide A accession
Q96QU1
Peptide B accession
Q96QU1
Peptide A residue number
268
Peptide B residue number
268

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 between cysteine 1392 of Protocadherin-15 and cysteine 35 of LHFPL tetraspan subfamily member 5 protein. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
6c14
Structure name
cryoem structure of mouse pcdh15-1ec-lhfpl5 complex
Structure deposition date
2018-01-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
81
Peptide A name
Protocadherin-15
Peptide B name
LHFPL tetraspan subfamily member 5 protein
Peptide A accession
Q99PJ1
Peptide B accession
Q4KL25
Peptide A residue number
1392
Peptide B residue number
35

Ligandability

Cysteine 1392 of Protocadherin-15

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 35 of LHFPL tetraspan subfamily member 5 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 between two units of Protocadherin-15 at cysteines 277 and 268 (256 and 247 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6e8f
Structure name
crystal structure of human protocadherin-15 ec3-5 cd2-1
Structure deposition date
2018-07-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide A name
Protocadherin-15
Peptide B name
Protocadherin-15
Peptide A accession
Q96QU1
Peptide B accession
Q96QU1
Peptide A residue number
277
Peptide B residue number
268

Ligandability

Cysteine 277 of Protocadherin-15

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 268 of Protocadherin-15

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 Protocadherin-15 between cysteines 273 and 282 (247 and 256 respectively in this structure).

Details

Redox score ?
89
PDB code
6cv7
Structure name
mouse protocadherin-15 extracellular cadherin domains 1 through 3
Structure deposition date
2018-03-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99PJ1
Residue number A
273
Residue number B
282
Peptide name
Protocadherin-15

Ligandability

Cysteine 273 of Protocadherin-15

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 282 of Protocadherin-15

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 Protocadherin-15 between cysteines 37 and 125 (11 and 99 respectively in this structure).

Details

Redox score ?
85
PDB code
6cv7
Structure name
mouse protocadherin-15 extracellular cadherin domains 1 through 3
Structure deposition date
2018-03-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99PJ1
Residue number A
37
Residue number B
125
Peptide name
Protocadherin-15

Ligandability

Cysteine 37 of Protocadherin-15

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 125 of Protocadherin-15

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 Protocadherin-15 between cysteines 1392 and 1393. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
6c14
Structure name
cryoem structure of mouse pcdh15-1ec-lhfpl5 complex
Structure deposition date
2018-01-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
72
Peptide accession
Q99PJ1
Residue number A
1392
Residue number B
1393
Peptide name
Protocadherin-15

Ligandability

Cysteine 1392 of Protocadherin-15

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 1393 of Protocadherin-15

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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