ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Glutaminase liver isoform, mitochondrial

Intramolecular
Cysteine 433 and cysteine 451
Cysteine 199 and cysteine 373
Cysteine 357 and cysteine 433
Cysteine 216 and cysteine 351
Cysteine 220 and cysteine 351
Cysteine 220 and cysteine 433
A redox-regulated disulphide may form within Glutaminase liver isoform, mitochondrial between cysteines 433 and 451.

Details

Redox score ?
65
PDB code
4bqm
Structure name
crystal structure of human liver-type glutaminase, catalytic domain
Structure deposition date
2013-05-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
97
Minimum pKa ?
9
% buried
100
Peptide accession
Q9UI32
Residue number A
433
Residue number B
451
Peptide name
Glutaminase liver isoform, mitochondrial

Ligandability

Cysteine 433 of Glutaminase liver isoform, mitochondrial

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 451 of Glutaminase liver isoform, mitochondrial

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 Glutaminase liver isoform, mitochondrial between cysteines 199 and 373. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
4bqm
Structure name
crystal structure of human liver-type glutaminase, catalytic domain
Structure deposition date
2013-05-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
60
Peptide accession
Q9UI32
Residue number A
199
Residue number B
373
Peptide name
Glutaminase liver isoform, mitochondrial

Ligandability

Cysteine 199 of Glutaminase liver isoform, mitochondrial

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 373 of Glutaminase liver isoform, mitochondrial

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 Glutaminase liver isoform, mitochondrial between cysteines 357 and 433. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
4bqm
Structure name
crystal structure of human liver-type glutaminase, catalytic domain
Structure deposition date
2013-05-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
100
Minimum pKa ?
13
% buried
99
Peptide accession
Q9UI32
Residue number A
357
Residue number B
433
Peptide name
Glutaminase liver isoform, mitochondrial

Ligandability

Cysteine 357 of Glutaminase liver isoform, mitochondrial

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 433 of Glutaminase liver isoform, mitochondrial

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 Glutaminase liver isoform, mitochondrial between cysteines 216 and 351. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
4bqm
Structure name
crystal structure of human liver-type glutaminase, catalytic domain
Structure deposition date
2013-05-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
10
% buried
86
Peptide accession
Q9UI32
Residue number A
216
Residue number B
351
Peptide name
Glutaminase liver isoform, mitochondrial

Ligandability

Cysteine 216 of Glutaminase liver isoform, mitochondrial

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 351 of Glutaminase liver isoform, mitochondrial

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 Glutaminase liver isoform, mitochondrial between cysteines 220 and 351. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
4bqm
Structure name
crystal structure of human liver-type glutaminase, catalytic domain
Structure deposition date
2013-05-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
92
Minimum pKa ?
11
% buried
100
Peptide accession
Q9UI32
Residue number A
220
Residue number B
351
Peptide name
Glutaminase liver isoform, mitochondrial

Ligandability

Cysteine 220 of Glutaminase liver isoform, mitochondrial

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 351 of Glutaminase liver isoform, mitochondrial

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 Glutaminase liver isoform, mitochondrial between cysteines 220 and 433. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
4bqm
Structure name
crystal structure of human liver-type glutaminase, catalytic domain
Structure deposition date
2013-05-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
100
Minimum pKa ?
11
% buried
100
Peptide accession
Q9UI32
Residue number A
220
Residue number B
433
Peptide name
Glutaminase liver isoform, mitochondrial

Ligandability

Cysteine 220 of Glutaminase liver isoform, mitochondrial

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 433 of Glutaminase liver isoform, mitochondrial

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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