ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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GMP synthase [glutamine-hydrolyzing]

Intermolecular
Cysteine 523 and cysteine 523
Intramolecular
Cysteine 530 and cysteine 554 L
Cysteine 226 and cysteine 252
Cysteine 489 and cysteine 554 L
A redox-regulated disulphide may form between two units of GMP synthase [glutamine-hydrolyzing] at cysteines 523 and 523. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2vxo
Structure name
human gmp synthetase in complex with xmp
Structure deposition date
2008-07-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
79
Peptide A name
GMP synthase [glutamine-hydrolyzing]
Peptide B name
GMP synthase [glutamine-hydrolyzing]
Peptide A accession
P49915
Peptide B accession
P49915
Peptide A residue number
523
Peptide B residue number
523

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 GMP synthase [glutamine-hydrolyzing] between cysteines 530 and 554. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
2vxo
Structure name
human gmp synthetase in complex with xmp
Structure deposition date
2008-07-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
91
Minimum pKa ?
12
% buried
100
Peptide accession
P49915
Residue number A
530
Residue number B
554
Peptide name
GMP synthase [glutamine-hydrolyzing]

Ligandability

Cysteine 530 of GMP synthase [glutamine-hydrolyzing]

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 554 of GMP synthase [glutamine-hydrolyzing]

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.

A redox-regulated disulphide may form within GMP synthase [glutamine-hydrolyzing] between cysteines 226 and 252. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
2vxo
Structure name
human gmp synthetase in complex with xmp
Structure deposition date
2008-07-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
96
Peptide accession
P49915
Residue number A
226
Residue number B
252
Peptide name
GMP synthase [glutamine-hydrolyzing]

Ligandability

Cysteine 226 of GMP synthase [glutamine-hydrolyzing]

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 252 of GMP synthase [glutamine-hydrolyzing]

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 GMP synthase [glutamine-hydrolyzing] between cysteines 489 and 554. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
2vxo
Structure name
human gmp synthetase in complex with xmp
Structure deposition date
2008-07-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
100
Peptide accession
P49915
Residue number A
489
Residue number B
554
Peptide name
GMP synthase [glutamine-hydrolyzing]

Ligandability

Cysteine 489 of GMP synthase [glutamine-hydrolyzing]

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 554 of GMP synthase [glutamine-hydrolyzing]

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.

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