Asparagine synthetase [glutamine-hydrolyzing]
Intermolecular
Cysteine 18 and cysteine 18
Intramolecular
Cysteine 115 and cysteine 207
Cysteine 13 and cysteine 44
Cysteine 13 and cysteine 43
Cysteine 43 and cysteine 44
Cysteine 2 and cysteine 73
Cysteine 13 and cysteine 18
Cysteine 18 and cysteine 44
Cysteine 73 and cysteine 158
6gq3 A 17 B 17
A redox-regulated disulphide may form between two units of Asparagine synthetase [glutamine-hydrolyzing] at cysteines 18 and 18 (17 and 17 respectively in this structure).
Details
Redox score ?
82
PDB code
6gq3
Structure name
human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1
Structure deposition date
2018-06-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide A name
Asparagine synthetase [glutamine-hydrolyzing]
Peptide B name
Asparagine synthetase [glutamine-hydrolyzing]
Peptide A accession
P08243
Peptide B accession
P08243
Peptide A residue number
18
Peptide B residue number
18
Ligandability
6gq3 B 114 B 206
A redox-regulated disulphide may form within Asparagine synthetase [glutamine-hydrolyzing] between cysteines 115 and 207 (114 and 206 respectively in this structure).
Details
Redox score ?
83
PDB code
6gq3
Structure name
human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1
Structure deposition date
2018-06-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08243
Residue number A
115
Residue number B
207
Peptide name
Asparagine synthetase [glutamine-hydrolyzing]
Ligandability
Cysteine 115 of Asparagine synthetase [glutamine-hydrolyzing]
Cysteine 207 of Asparagine synthetase [glutamine-hydrolyzing]
6gq3 B 12 B 43
A redox-regulated disulphide may form within Asparagine synthetase [glutamine-hydrolyzing] between cysteines 13 and 44 (12 and 43 respectively in this structure).
Details
Redox score ?
81
PDB code
6gq3
Structure name
human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1
Structure deposition date
2018-06-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08243
Residue number A
13
Residue number B
44
Peptide name
Asparagine synthetase [glutamine-hydrolyzing]
Ligandability
Cysteine 13 of Asparagine synthetase [glutamine-hydrolyzing]
Cysteine 44 of Asparagine synthetase [glutamine-hydrolyzing]
6gq3 B 12 B 42
A redox-regulated disulphide may form within Asparagine synthetase [glutamine-hydrolyzing] between cysteines 13 and 43 (12 and 42 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
6gq3
Structure name
human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1
Structure deposition date
2018-06-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
nan
Peptide accession
P08243
Residue number A
13
Residue number B
43
Peptide name
Asparagine synthetase [glutamine-hydrolyzing]
Ligandability
Cysteine 13 of Asparagine synthetase [glutamine-hydrolyzing]
Cysteine 43 of Asparagine synthetase [glutamine-hydrolyzing]
6gq3 A 42 A 43
A redox-regulated disulphide may form within Asparagine synthetase [glutamine-hydrolyzing] between cysteines 43 and 44 (42 and 43 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
6gq3
Structure name
human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1
Structure deposition date
2018-06-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
nan
Peptide accession
P08243
Residue number A
43
Residue number B
44
Peptide name
Asparagine synthetase [glutamine-hydrolyzing]
Ligandability
Cysteine 43 of Asparagine synthetase [glutamine-hydrolyzing]
Cysteine 44 of Asparagine synthetase [glutamine-hydrolyzing]
6gq3 A 1 A 72
A redox-regulated disulphide may form within Asparagine synthetase [glutamine-hydrolyzing] between cysteines 2 and 73 (1 and 72 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
6gq3
Structure name
human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1
Structure deposition date
2018-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
13
% buried
nan
Peptide accession
P08243
Residue number A
2
Residue number B
73
Peptide name
Asparagine synthetase [glutamine-hydrolyzing]
Ligandability
Cysteine 2 of Asparagine synthetase [glutamine-hydrolyzing]
Cysteine 73 of Asparagine synthetase [glutamine-hydrolyzing]
6gq3 B 12 B 17
A redox-regulated disulphide may form within Asparagine synthetase [glutamine-hydrolyzing] between cysteines 13 and 18 (12 and 17 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
6gq3
Structure name
human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1
Structure deposition date
2018-06-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08243
Residue number A
13
Residue number B
18
Peptide name
Asparagine synthetase [glutamine-hydrolyzing]
Ligandability
Cysteine 13 of Asparagine synthetase [glutamine-hydrolyzing]
Cysteine 18 of Asparagine synthetase [glutamine-hydrolyzing]
6gq3 B 17 B 43
A redox-regulated disulphide may form within Asparagine synthetase [glutamine-hydrolyzing] between cysteines 18 and 44 (17 and 43 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
6gq3
Structure name
human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1
Structure deposition date
2018-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08243
Residue number A
18
Residue number B
44
Peptide name
Asparagine synthetase [glutamine-hydrolyzing]
Ligandability
Cysteine 18 of Asparagine synthetase [glutamine-hydrolyzing]
Cysteine 44 of Asparagine synthetase [glutamine-hydrolyzing]
6gq3 B 72 B 157
A redox-regulated disulphide may form within Asparagine synthetase [glutamine-hydrolyzing] between cysteines 73 and 158 (72 and 157 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
23
PDB code
6gq3
Structure name
human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1
Structure deposition date
2018-06-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
94
Minimum pKa ?
13
% buried
100
Peptide accession
P08243
Residue number A
73
Residue number B
158
Peptide name
Asparagine synthetase [glutamine-hydrolyzing]
Ligandability
Cysteine 73 of Asparagine synthetase [glutamine-hydrolyzing]
Cysteine 158 of Asparagine synthetase [glutamine-hydrolyzing]
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