Glutamine-dependent NAD(+) synthetase
Intramolecular
Cysteine 367 and cysteine 554
Cysteine 373 and cysteine 409
Cysteine 49 and cysteine 53
Cysteine 374 and cysteine 377
Cysteine 373 and cysteine 377
Cysteine 373 and cysteine 374
Cysteine 374 and cysteine 409
Cysteine 377 and cysteine 409
Cysteine 416 and cysteine 531
Cysteine 617 and cysteine 686
More...Cysteine 367 and cysteine 409
Cysteine 374 and cysteine 554
Cysteine 10 and cysteine 84
6ofb A 367 A 554
A redox-regulated disulphide may form within Glutamine-dependent NAD(+) synthetase between cysteines 367 and 554.
Details
Redox score ?
70
PDB code
6ofb
Structure name
crystal structure of human glutamine-dependent nad+ synthetase complexed with naad+, amp, pyrophosphate, and mg2+
Structure deposition date
2019-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
96
Peptide accession
Q6IA69
Residue number A
367
Residue number B
554
Peptide name
Glutamine-dependent NAD(+) synthetase
Ligandability
Cysteine 367 of Glutamine-dependent NAD(+) synthetase
Cysteine 554 of Glutamine-dependent NAD(+) synthetase
6ofb B 373 B 409
A redox-regulated disulphide may form within Glutamine-dependent NAD(+) synthetase between cysteines 373 and 409.
Details
Redox score ?
68
PDB code
6ofb
Structure name
crystal structure of human glutamine-dependent nad+ synthetase complexed with naad+, amp, pyrophosphate, and mg2+
Structure deposition date
2019-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
9
% buried
99
Peptide accession
Q6IA69
Residue number A
373
Residue number B
409
Peptide name
Glutamine-dependent NAD(+) synthetase
Ligandability
Cysteine 373 of Glutamine-dependent NAD(+) synthetase
Cysteine 409 of Glutamine-dependent NAD(+) synthetase
6ofb A 49 A 53
A redox-regulated disulphide may form within Glutamine-dependent NAD(+) synthetase between cysteines 49 and 53.
Details
Redox score ?
67
PDB code
6ofb
Structure name
crystal structure of human glutamine-dependent nad+ synthetase complexed with naad+, amp, pyrophosphate, and mg2+
Structure deposition date
2019-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
88
Minimum pKa ?
8
% buried
100
Peptide accession
Q6IA69
Residue number A
49
Residue number B
53
Peptide name
Glutamine-dependent NAD(+) synthetase
Ligandability
Cysteine 49 of Glutamine-dependent NAD(+) synthetase
Cysteine 53 of Glutamine-dependent NAD(+) synthetase
6ofb A 374 A 377
A redox-regulated disulphide may form within Glutamine-dependent NAD(+) synthetase between cysteines 374 and 377. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
6ofb
Structure name
crystal structure of human glutamine-dependent nad+ synthetase complexed with naad+, amp, pyrophosphate, and mg2+
Structure deposition date
2019-03-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
67
Peptide accession
Q6IA69
Residue number A
374
Residue number B
377
Peptide name
Glutamine-dependent NAD(+) synthetase
Ligandability
Cysteine 374 of Glutamine-dependent NAD(+) synthetase
Cysteine 377 of Glutamine-dependent NAD(+) synthetase
6ofb A 373 A 377
A redox-regulated disulphide may form within Glutamine-dependent NAD(+) synthetase between cysteines 373 and 377. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
6ofb
Structure name
crystal structure of human glutamine-dependent nad+ synthetase complexed with naad+, amp, pyrophosphate, and mg2+
Structure deposition date
2019-03-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
69
Minimum pKa ?
12
% buried
78
Peptide accession
Q6IA69
Residue number A
373
Residue number B
377
Peptide name
Glutamine-dependent NAD(+) synthetase
Ligandability
Cysteine 373 of Glutamine-dependent NAD(+) synthetase
Cysteine 377 of Glutamine-dependent NAD(+) synthetase
6ofb B 373 B 374
A redox-regulated disulphide may form within Glutamine-dependent NAD(+) synthetase between cysteines 373 and 374. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
6ofb
Structure name
crystal structure of human glutamine-dependent nad+ synthetase complexed with naad+, amp, pyrophosphate, and mg2+
Structure deposition date
2019-03-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
88
Peptide accession
Q6IA69
Residue number A
373
Residue number B
374
Peptide name
Glutamine-dependent NAD(+) synthetase
Ligandability
Cysteine 373 of Glutamine-dependent NAD(+) synthetase
Cysteine 374 of Glutamine-dependent NAD(+) synthetase
6ofb A 374 A 409
A redox-regulated disulphide may form within Glutamine-dependent NAD(+) synthetase between cysteines 374 and 409. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
6ofb
Structure name
crystal structure of human glutamine-dependent nad+ synthetase complexed with naad+, amp, pyrophosphate, and mg2+
Structure deposition date
2019-03-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
88
Peptide accession
Q6IA69
Residue number A
374
Residue number B
409
Peptide name
Glutamine-dependent NAD(+) synthetase
Ligandability
Cysteine 374 of Glutamine-dependent NAD(+) synthetase
Cysteine 409 of Glutamine-dependent NAD(+) synthetase
6ofb B 377 B 409
A redox-regulated disulphide may form within Glutamine-dependent NAD(+) synthetase between cysteines 377 and 409. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
6ofb
Structure name
crystal structure of human glutamine-dependent nad+ synthetase complexed with naad+, amp, pyrophosphate, and mg2+
Structure deposition date
2019-03-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
9
% buried
76
Peptide accession
Q6IA69
Residue number A
377
Residue number B
409
Peptide name
Glutamine-dependent NAD(+) synthetase
Ligandability
Cysteine 377 of Glutamine-dependent NAD(+) synthetase
Cysteine 409 of Glutamine-dependent NAD(+) synthetase
6ofb B 416 B 531
A redox-regulated disulphide may form within Glutamine-dependent NAD(+) synthetase between cysteines 416 and 531. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
6ofb
Structure name
crystal structure of human glutamine-dependent nad+ synthetase complexed with naad+, amp, pyrophosphate, and mg2+
Structure deposition date
2019-03-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
100
Peptide accession
Q6IA69
Residue number A
416
Residue number B
531
Peptide name
Glutamine-dependent NAD(+) synthetase
Ligandability
Cysteine 416 of Glutamine-dependent NAD(+) synthetase
Cysteine 531 of Glutamine-dependent NAD(+) synthetase
6ofb A 617 A 686
A redox-regulated disulphide may form within Glutamine-dependent NAD(+) synthetase between cysteines 617 and 686. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
6ofb
Structure name
crystal structure of human glutamine-dependent nad+ synthetase complexed with naad+, amp, pyrophosphate, and mg2+
Structure deposition date
2019-03-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
56
Peptide accession
Q6IA69
Residue number A
617
Residue number B
686
Peptide name
Glutamine-dependent NAD(+) synthetase
Ligandability
Cysteine 617 of Glutamine-dependent NAD(+) synthetase
Cysteine 686 of Glutamine-dependent NAD(+) synthetase
6ofb B 367 B 409
A redox-regulated disulphide may form within Glutamine-dependent NAD(+) synthetase between cysteines 367 and 409. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
6ofb
Structure name
crystal structure of human glutamine-dependent nad+ synthetase complexed with naad+, amp, pyrophosphate, and mg2+
Structure deposition date
2019-03-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
9
% buried
99
Peptide accession
Q6IA69
Residue number A
367
Residue number B
409
Peptide name
Glutamine-dependent NAD(+) synthetase
Ligandability
Cysteine 367 of Glutamine-dependent NAD(+) synthetase
Cysteine 409 of Glutamine-dependent NAD(+) synthetase
6ofb A 374 A 554
A redox-regulated disulphide may form within Glutamine-dependent NAD(+) synthetase between cysteines 374 and 554. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
6ofb
Structure name
crystal structure of human glutamine-dependent nad+ synthetase complexed with naad+, amp, pyrophosphate, and mg2+
Structure deposition date
2019-03-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
84
Peptide accession
Q6IA69
Residue number A
374
Residue number B
554
Peptide name
Glutamine-dependent NAD(+) synthetase
Ligandability
Cysteine 374 of Glutamine-dependent NAD(+) synthetase
Cysteine 554 of Glutamine-dependent NAD(+) synthetase
6ofb B 10 B 84
A redox-regulated disulphide may form within Glutamine-dependent NAD(+) synthetase between cysteines 10 and 84. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
23
PDB code
6ofb
Structure name
crystal structure of human glutamine-dependent nad+ synthetase complexed with naad+, amp, pyrophosphate, and mg2+
Structure deposition date
2019-03-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
102
Minimum pKa ?
11
% buried
100
Peptide accession
Q6IA69
Residue number A
10
Residue number B
84
Peptide name
Glutamine-dependent NAD(+) synthetase
Ligandability
Cysteine 10 of Glutamine-dependent NAD(+) synthetase
Cysteine 84 of Glutamine-dependent NAD(+) synthetase
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