ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Polypeptide N-acetylgalactosaminyltransferase 1

Intramolecular
Cysteine 330 and cysteine 408
Cysteine 442 and cysteine 459
Cysteine 482 and cysteine 497
Cysteine 523 and cysteine 540
Cysteine 106 and cysteine 339
Cysteine 212 and cysteine 214
A redox-regulated disulphide may form within Polypeptide N-acetylgalactosaminyltransferase 1 between cysteines 330 and 408.

Details

Redox score ?
86
PDB code
1xhb
Structure name
the crystal structure of udp-galnac: polypeptide alpha-n- acetylgalactosaminyltransferase-t1
Structure deposition date
2004-09-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08912
Residue number A
330
Residue number B
408
Peptide name
Polypeptide N-acetylgalactosaminyltransferase 1

Ligandability

Cysteine 330 of Polypeptide N-acetylgalactosaminyltransferase 1

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 408 of Polypeptide N-acetylgalactosaminyltransferase 1

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 Polypeptide N-acetylgalactosaminyltransferase 1 between cysteines 442 and 459.

Details

Redox score ?
84
PDB code
1xhb
Structure name
the crystal structure of udp-galnac: polypeptide alpha-n- acetylgalactosaminyltransferase-t1
Structure deposition date
2004-09-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08912
Residue number A
442
Residue number B
459
Peptide name
Polypeptide N-acetylgalactosaminyltransferase 1

Ligandability

Cysteine 442 of Polypeptide N-acetylgalactosaminyltransferase 1

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 459 of Polypeptide N-acetylgalactosaminyltransferase 1

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 Polypeptide N-acetylgalactosaminyltransferase 1 between cysteines 482 and 497.

Details

Redox score ?
84
PDB code
1xhb
Structure name
the crystal structure of udp-galnac: polypeptide alpha-n- acetylgalactosaminyltransferase-t1
Structure deposition date
2004-09-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08912
Residue number A
482
Residue number B
497
Peptide name
Polypeptide N-acetylgalactosaminyltransferase 1

Ligandability

Cysteine 482 of Polypeptide N-acetylgalactosaminyltransferase 1

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 497 of Polypeptide N-acetylgalactosaminyltransferase 1

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 Polypeptide N-acetylgalactosaminyltransferase 1 between cysteines 523 and 540.

Details

Redox score ?
83
PDB code
1xhb
Structure name
the crystal structure of udp-galnac: polypeptide alpha-n- acetylgalactosaminyltransferase-t1
Structure deposition date
2004-09-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08912
Residue number A
523
Residue number B
540
Peptide name
Polypeptide N-acetylgalactosaminyltransferase 1

Ligandability

Cysteine 523 of Polypeptide N-acetylgalactosaminyltransferase 1

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 540 of Polypeptide N-acetylgalactosaminyltransferase 1

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 Polypeptide N-acetylgalactosaminyltransferase 1 between cysteines 106 and 339.

Details

Redox score ?
83
PDB code
1xhb
Structure name
the crystal structure of udp-galnac: polypeptide alpha-n- acetylgalactosaminyltransferase-t1
Structure deposition date
2004-09-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
O08912
Residue number A
106
Residue number B
339
Peptide name
Polypeptide N-acetylgalactosaminyltransferase 1

Ligandability

Cysteine 106 of Polypeptide N-acetylgalactosaminyltransferase 1

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 339 of Polypeptide N-acetylgalactosaminyltransferase 1

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 Polypeptide N-acetylgalactosaminyltransferase 1 between cysteines 212 and 214. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
1xhb
Structure name
the crystal structure of udp-galnac: polypeptide alpha-n- acetylgalactosaminyltransferase-t1
Structure deposition date
2004-09-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
100
Peptide accession
O08912
Residue number A
212
Residue number B
214
Peptide name
Polypeptide N-acetylgalactosaminyltransferase 1

Ligandability

Cysteine 212 of Polypeptide N-acetylgalactosaminyltransferase 1

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 214 of Polypeptide N-acetylgalactosaminyltransferase 1

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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