ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2

Intramolecular
Cysteine 66 and cysteine 148
Cysteine 151 and cysteine 317
Cysteine 148 and cysteine 317
Cysteine 148 and cysteine 151
A redox-regulated disulphide may form within Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 between cysteines 66 and 148.

Details

Redox score ?
89
PDB code
6apl
Structure name
crystal structure of human st6galnac2 in complex with cmp
Structure deposition date
2017-08-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UJ37
Residue number A
66
Residue number B
148
Peptide name
Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2

Ligandability

Cysteine 66 of Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 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 148 of Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 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 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 between cysteines 151 and 317.

Details

Redox score ?
82
PDB code
6apl
Structure name
crystal structure of human st6galnac2 in complex with cmp
Structure deposition date
2017-08-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UJ37
Residue number A
151
Residue number B
317
Peptide name
Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2

Ligandability

Cysteine 151 of Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 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 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 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 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 between cysteines 148 and 317. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
6apj
Structure name
crystal structure of human st6galnac2
Structure deposition date
2017-08-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UJ37
Residue number A
148
Residue number B
317
Peptide name
Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2

Ligandability

Cysteine 148 of Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 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 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 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 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 between cysteines 148 and 151. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6apl
Structure name
crystal structure of human st6galnac2 in complex with cmp
Structure deposition date
2017-08-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UJ37
Residue number A
148
Residue number B
151
Peptide name
Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2

Ligandability

Cysteine 148 of Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 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 151 of Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 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: