ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

Intramolecular
Cysteine 845 and cysteine 921 L
Cysteine 297 and cysteine 323 L
Cysteine 297 and cysteine 315
Cysteine 267 and cysteine 297
A redox-regulated disulphide may form within UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit between cysteines 845 and 921 (835 and 911 respectively in this structure).

Details

Redox score ?
63
PDB code
5vif
Structure name
electrophilic probes for deciphering substrate recognition by o-glcnac transferase
Structure deposition date
2017-04-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
86
Minimum pKa ?
9
% buried
100
Peptide accession
O15294
Residue number A
845
Residue number B
921
Peptide name
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

Ligandability

Cysteine 845 of UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 921 of UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

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 UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit between cysteines 297 and 323 (287 and 313 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
1w3b
Structure name
the superhelical tpr domain of o-linked glcnac transferase reveals structural similarities to importin alpha
Structure deposition date
2004-07-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
10
Peptide accession
O15294
Residue number A
297
Residue number B
323
Peptide name
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

Ligandability

Cysteine 297 of UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

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 323 of UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

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 UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit between cysteines 297 and 315. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
6eou
Structure name
o-glcnac transferase tpr domain with the intellectual disability associated mutation l254f
Structure deposition date
2017-10-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
67
Peptide accession
O15294
Residue number A
297
Residue number B
315
Peptide name
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

Ligandability

Cysteine 297 of UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

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 315 of UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

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 UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit between cysteines 267 and 297 (257 and 287 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
1w3b
Structure name
the superhelical tpr domain of o-linked glcnac transferase reveals structural similarities to importin alpha
Structure deposition date
2004-07-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
10
% buried
76
Peptide accession
O15294
Residue number A
267
Residue number B
297
Peptide name
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

Ligandability

Cysteine 267 of UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

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 297 of UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

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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