ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase

Intermolecular
Cysteine 172 and cysteine 172
Intramolecular
Cysteine 579 and cysteine 581
Cysteine 579 and cysteine 586
Cysteine 581 and cysteine 586
A redox-regulated disulphide may form between two units of Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase at cysteines 172 and 172.

Details

Redox score ?
73
PDB code
4zht
Structure name
crystal structure of udp-glcnac 2-epimerase
Structure deposition date
2015-04-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
7
% buried
70
Peptide A name
Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
Peptide B name
Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
Peptide A accession
Q9Y223
Peptide B accession
Q9Y223
Peptide A residue number
172
Peptide B residue number
172

Ligandability

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 Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase between cysteines 579 and 581.

Details

Redox score ?
82
PDB code
3eo3
Structure name
crystal structure of the n-acetylmannosamine kinase domain of human gne protein
Structure deposition date
2008-09-26
Thiol separation (Å)
3
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y223
Residue number A
579
Residue number B
581
Peptide name
Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase

Ligandability

Cysteine 579 of Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase

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 581 of Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase

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 Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase between cysteines 579 and 586.

Details

Redox score ?
77
PDB code
3eo3
Structure name
crystal structure of the n-acetylmannosamine kinase domain of human gne protein
Structure deposition date
2008-09-26
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y223
Residue number A
579
Residue number B
586
Peptide name
Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase

Ligandability

Cysteine 579 of Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase

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 586 of Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase

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 Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase between cysteines 581 and 586.

Details

Redox score ?
72
PDB code
3eo3
Structure name
crystal structure of the n-acetylmannosamine kinase domain of human gne protein
Structure deposition date
2008-09-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y223
Residue number A
581
Residue number B
586
Peptide name
Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase

Ligandability

Cysteine 581 of Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase

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 586 of Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase

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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