ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2

Intramolecular
Cysteine 367 and cysteine 397
Cysteine 138 and cysteine 235
Cysteine 96 and cysteine 125
A redox-regulated disulphide may form within N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2 between cysteines 367 and 397.

Details

Redox score ?
89
PDB code
6wmn
Structure name
human poly-n-acetyl-lactosamine synthase structure demonstrates a modular assembly of catalytic subsites for gt-a glycosyltransferases
Structure deposition date
2020-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NY97
Residue number A
367
Residue number B
397
Peptide name
N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2

Ligandability

Cysteine 367 of N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 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 397 of N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 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 N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2 between cysteines 138 and 235.

Details

Redox score ?
86
PDB code
6wmo
Structure name
human poly-n-acetyl-lactosamine synthase structure demonstrates a modular assembly of catalytic subsites for gt-a glycosyltransferases
Structure deposition date
2020-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NY97
Residue number A
138
Residue number B
235
Peptide name
N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2

Ligandability

Cysteine 138 of N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 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 235 of N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 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 N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2 between cysteines 96 and 125.

Details

Redox score ?
84
PDB code
6wmn
Structure name
human poly-n-acetyl-lactosamine synthase structure demonstrates a modular assembly of catalytic subsites for gt-a glycosyltransferases
Structure deposition date
2020-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NY97
Residue number A
96
Residue number B
125
Peptide name
N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2

Ligandability

Cysteine 96 of N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 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 125 of N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 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.

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