ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Syncytin-2

Intramolecular
Cysteine 200 and cysteine 253
Cysteine 126 and cysteine 145
Cysteine 431 and cysteine 438
Cysteine 301 and cysteine 317
Cysteine 291 and cysteine 308
Cysteine 438 and cysteine 439
Cysteine 431 and cysteine 439
Cysteine 193 and cysteine 215
Cysteine 126 and cysteine 317
A redox-regulated disulphide may form within Syncytin-2 between cysteines 200 and 253.

Details

Redox score ?
87
PDB code
7oix
Structure name
structure of thermostable human mfsd2a in complex with thermostable human sync2
Structure deposition date
2021-05-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P60508
Residue number A
200
Residue number B
253
Peptide name
Syncytin-2

Ligandability

Cysteine 200 of Syncytin-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 253 of Syncytin-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 Syncytin-2 between cysteines 126 and 145.

Details

Redox score ?
85
PDB code
7oix
Structure name
structure of thermostable human mfsd2a in complex with thermostable human sync2
Structure deposition date
2021-05-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P60508
Residue number A
126
Residue number B
145
Peptide name
Syncytin-2

Ligandability

Cysteine 126 of Syncytin-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 145 of Syncytin-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 Syncytin-2 between cysteines 431 and 438.

Details

Redox score ?
84
PDB code
6rx3
Structure name
crystal structure of human syncytin 2 in post-fusion conformation
Structure deposition date
2019-06-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P60508
Residue number A
431
Residue number B
438
Peptide name
Syncytin-2

Ligandability

Cysteine 431 of Syncytin-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 438 of Syncytin-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 Syncytin-2 between cysteines 301 and 317.

Details

Redox score ?
78
PDB code
7oix
Structure name
structure of thermostable human mfsd2a in complex with thermostable human sync2
Structure deposition date
2021-05-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
92
Minimum pKa ?
nan
% buried
nan
Peptide accession
P60508
Residue number A
301
Residue number B
317
Peptide name
Syncytin-2

Ligandability

Cysteine 301 of Syncytin-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 317 of Syncytin-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 Syncytin-2 between cysteines 291 and 308.

Details

Redox score ?
78
PDB code
7oix
Structure name
structure of thermostable human mfsd2a in complex with thermostable human sync2
Structure deposition date
2021-05-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P60508
Residue number A
291
Residue number B
308
Peptide name
Syncytin-2

Ligandability

Cysteine 291 of Syncytin-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 308 of Syncytin-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 Syncytin-2 between cysteines 438 and 439. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
6rx3
Structure name
crystal structure of human syncytin 2 in post-fusion conformation
Structure deposition date
2019-06-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
48
Minimum pKa ?
10
% buried
nan
Peptide accession
P60508
Residue number A
438
Residue number B
439
Peptide name
Syncytin-2

Ligandability

Cysteine 438 of Syncytin-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 439 of Syncytin-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 Syncytin-2 between cysteines 431 and 439. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
6rx3
Structure name
crystal structure of human syncytin 2 in post-fusion conformation
Structure deposition date
2019-06-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
nan
Peptide accession
P60508
Residue number A
431
Residue number B
439
Peptide name
Syncytin-2

Ligandability

Cysteine 431 of Syncytin-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 439 of Syncytin-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 Syncytin-2 between cysteines 193 and 215. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
7oix
Structure name
structure of thermostable human mfsd2a in complex with thermostable human sync2
Structure deposition date
2021-05-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
32
Peptide accession
P60508
Residue number A
193
Residue number B
215
Peptide name
Syncytin-2

Ligandability

Cysteine 193 of Syncytin-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 215 of Syncytin-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 Syncytin-2 between cysteines 126 and 317. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
7oix
Structure name
structure of thermostable human mfsd2a in complex with thermostable human sync2
Structure deposition date
2021-05-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
P60508
Residue number A
126
Residue number B
317
Peptide name
Syncytin-2

Ligandability

Cysteine 126 of Syncytin-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 317 of Syncytin-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.

If this tool was useful for finding a disulphide, please cite: