ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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N-acylglucosamine 2-epimerase

Intramolecular
Cysteine 386 and cysteine 390
Cysteine 239 and cysteine 302
Cysteine 125 and cysteine 210
Cysteine 104 and cysteine 125
A redox-regulated disulphide may form within N-acylglucosamine 2-epimerase between cysteines 386 and 390.

Details

Redox score ?
63
PDB code
1fp3
Structure name
crystal structure of n-acyl-d-glucosamine 2-epimerase from porcine kidney
Structure deposition date
2000-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
9
% buried
100
Peptide accession
P17560
Residue number A
386
Residue number B
390
Peptide name
N-acylglucosamine 2-epimerase

Ligandability

Cysteine 386 of N-acylglucosamine 2-epimerase

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 390 of N-acylglucosamine 2-epimerase

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-acylglucosamine 2-epimerase between cysteines 239 and 302. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
1fp3
Structure name
crystal structure of n-acyl-d-glucosamine 2-epimerase from porcine kidney
Structure deposition date
2000-08-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
42
Minimum pKa ?
9
% buried
0
Peptide accession
P17560
Residue number A
239
Residue number B
302
Peptide name
N-acylglucosamine 2-epimerase

Ligandability

Cysteine 239 of N-acylglucosamine 2-epimerase

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 302 of N-acylglucosamine 2-epimerase

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-acylglucosamine 2-epimerase between cysteines 125 and 210. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
1fp3
Structure name
crystal structure of n-acyl-d-glucosamine 2-epimerase from porcine kidney
Structure deposition date
2000-08-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
98
Peptide accession
P17560
Residue number A
125
Residue number B
210
Peptide name
N-acylglucosamine 2-epimerase

Ligandability

Cysteine 125 of N-acylglucosamine 2-epimerase

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 210 of N-acylglucosamine 2-epimerase

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-acylglucosamine 2-epimerase between cysteines 104 and 125. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
22
PDB code
1fp3
Structure name
crystal structure of n-acyl-d-glucosamine 2-epimerase from porcine kidney
Structure deposition date
2000-08-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
92
Minimum pKa ?
13
% buried
100
Peptide accession
P17560
Residue number A
104
Residue number B
125
Peptide name
N-acylglucosamine 2-epimerase

Ligandability

Cysteine 104 of N-acylglucosamine 2-epimerase

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-acylglucosamine 2-epimerase

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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