Protein lin-54 homolog
Intramolecular
Cysteine 601 and cysteine 611
Cysteine 611 and cysteine 620
Cysteine 599 and cysteine 611
Cysteine 624 and cysteine 626
Cysteine 606 and cysteine 611
Cysteine 620 and cysteine 626
Cysteine 620 and cysteine 624
Cysteine 613 and cysteine 624
Cysteine 546 and cysteine 549
Cysteine 599 and cysteine 626
More...Cysteine 546 and cysteine 551
Cysteine 611 and cysteine 613
Cysteine 599 and cysteine 624
Cysteine 539 and cysteine 549
Cysteine 525 and cysteine 546
Cysteine 546 and cysteine 554
Cysteine 525 and cysteine 549
Cysteine 626 and cysteine 629
Cysteine 620 and cysteine 629
Cysteine 539 and cysteine 546
Cysteine 532 and cysteine 546
Cysteine 551 and cysteine 554
Cysteine 599 and cysteine 620
Cysteine 599 and cysteine 601
Cysteine 525 and cysteine 551
Cysteine 611 and cysteine 626
Cysteine 537 and cysteine 546
Cysteine 549 and cysteine 551
Cysteine 611 and cysteine 624
Cysteine 599 and cysteine 606
Cysteine 525 and cysteine 527
Cysteine 599 and cysteine 613
Cysteine 606 and cysteine 629
Cysteine 525 and cysteine 532
Cysteine 525 and cysteine 539
Cysteine 525 and cysteine 537
Cysteine 611 and cysteine 629
Cysteine 606 and cysteine 626
Cysteine 532 and cysteine 551
Cysteine 532 and cysteine 554
5fd3 A 601 A 611
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 601 and 611.
Details
Redox score ?
95
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
2
% buried
50
Peptide accession
Q6MZP7
Residue number A
601
Residue number B
611
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 601 of Protein lin-54 homolog
Cysteine 611 of Protein lin-54 homolog
5fd3 A 611 A 620
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 611 and 620.
Details
Redox score ?
92
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
2
% buried
38
Peptide accession
Q6MZP7
Residue number A
611
Residue number B
620
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 611 of Protein lin-54 homolog
Cysteine 620 of Protein lin-54 homolog
5fd3 B 599 B 611
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 599 and 611.
Details
Redox score ?
92
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
3
% buried
41
Peptide accession
Q6MZP7
Residue number A
599
Residue number B
611
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 599 of Protein lin-54 homolog
Cysteine 611 of Protein lin-54 homolog
5fd3 B 624 B 626
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 624 and 626.
Details
Redox score ?
91
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
5
% buried
16
Peptide accession
Q6MZP7
Residue number A
624
Residue number B
626
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 624 of Protein lin-54 homolog
Cysteine 626 of Protein lin-54 homolog
5fd3 B 606 B 611
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 606 and 611.
Details
Redox score ?
91
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
3
% buried
46
Peptide accession
Q6MZP7
Residue number A
606
Residue number B
611
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 606 of Protein lin-54 homolog
Cysteine 611 of Protein lin-54 homolog
5fd3 A 620 A 626
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 620 and 626.
Details
Redox score ?
91
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
60
Minimum pKa ?
6
% buried
24
Peptide accession
Q6MZP7
Residue number A
620
Residue number B
626
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 620 of Protein lin-54 homolog
Cysteine 626 of Protein lin-54 homolog
5fd3 B 620 B 624
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 620 and 624.
Details
Redox score ?
91
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
5
% buried
21
Peptide accession
Q6MZP7
Residue number A
620
Residue number B
624
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 620 of Protein lin-54 homolog
Cysteine 624 of Protein lin-54 homolog
5fd3 A 613 A 624
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 613 and 624.
Details
Redox score ?
90
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
12
Peptide accession
Q6MZP7
Residue number A
613
Residue number B
624
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 613 of Protein lin-54 homolog
Cysteine 624 of Protein lin-54 homolog
5fd3 A 546 A 549
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 546 and 549.
Details
Redox score ?
89
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
5
% buried
28
Peptide accession
Q6MZP7
Residue number A
546
Residue number B
549
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 546 of Protein lin-54 homolog
Cysteine 549 of Protein lin-54 homolog
5fd3 B 599 B 626
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 599 and 626.
Details
Redox score ?
88
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
57
Minimum pKa ?
7
% buried
26
Peptide accession
Q6MZP7
Residue number A
599
Residue number B
626
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 599 of Protein lin-54 homolog
Cysteine 626 of Protein lin-54 homolog
5fd3 B 546 B 551
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 546 and 551.
Details
Redox score ?
88
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
5
% buried
40
Peptide accession
Q6MZP7
Residue number A
546
Residue number B
551
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 546 of Protein lin-54 homolog
Cysteine 551 of Protein lin-54 homolog
5fd3 B 611 B 613
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 611 and 613.
Details
Redox score ?
88
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
3
% buried
36
Peptide accession
Q6MZP7
Residue number A
611
Residue number B
613
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 611 of Protein lin-54 homolog
Cysteine 613 of Protein lin-54 homolog
5fd3 A 599 A 624
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 599 and 624.
Details
Redox score ?
87
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
6
% buried
17
Peptide accession
Q6MZP7
Residue number A
599
Residue number B
624
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 599 of Protein lin-54 homolog
Cysteine 624 of Protein lin-54 homolog
5fd3 A 539 A 549
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 539 and 549.
Details
Redox score ?
87
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
58
Minimum pKa ?
6
% buried
25
Peptide accession
Q6MZP7
Residue number A
539
Residue number B
549
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 539 of Protein lin-54 homolog
Cysteine 549 of Protein lin-54 homolog
5fd3 B 525 B 546
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 525 and 546.
Details
Redox score ?
87
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
5
% buried
44
Peptide accession
Q6MZP7
Residue number A
525
Residue number B
546
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 525 of Protein lin-54 homolog
Cysteine 546 of Protein lin-54 homolog
5fd3 B 546 B 554
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 546 and 554.
Details
Redox score ?
86
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
5
% buried
44
Peptide accession
Q6MZP7
Residue number A
546
Residue number B
554
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 546 of Protein lin-54 homolog
Cysteine 554 of Protein lin-54 homolog
5fd3 B 525 B 549
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 525 and 549.
Details
Redox score ?
86
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
27
Peptide accession
Q6MZP7
Residue number A
525
Residue number B
549
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 525 of Protein lin-54 homolog
Cysteine 549 of Protein lin-54 homolog
5fd3 B 626 B 629
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 626 and 629.
Details
Redox score ?
86
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
6
% buried
26
Peptide accession
Q6MZP7
Residue number A
626
Residue number B
629
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 626 of Protein lin-54 homolog
Cysteine 629 of Protein lin-54 homolog
5fd3 B 620 B 629
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 620 and 629.
Details
Redox score ?
86
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
64
Minimum pKa ?
6
% buried
30
Peptide accession
Q6MZP7
Residue number A
620
Residue number B
629
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 620 of Protein lin-54 homolog
Cysteine 629 of Protein lin-54 homolog
5fd3 A 539 A 546
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 539 and 546.
Details
Redox score ?
85
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
5
% buried
38
Peptide accession
Q6MZP7
Residue number A
539
Residue number B
546
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 539 of Protein lin-54 homolog
Cysteine 546 of Protein lin-54 homolog
5fd3 B 532 B 546
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 532 and 546.
Details
Redox score ?
84
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
5
% buried
53
Peptide accession
Q6MZP7
Residue number A
532
Residue number B
546
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 532 of Protein lin-54 homolog
Cysteine 546 of Protein lin-54 homolog
5fd3 A 551 A 554
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 551 and 554.
Details
Redox score ?
84
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
8
% buried
28
Peptide accession
Q6MZP7
Residue number A
551
Residue number B
554
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 551 of Protein lin-54 homolog
Cysteine 554 of Protein lin-54 homolog
5fd3 B 599 B 620
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 599 and 620.
Details
Redox score ?
84
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
7
% buried
30
Peptide accession
Q6MZP7
Residue number A
599
Residue number B
620
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 599 of Protein lin-54 homolog
Cysteine 620 of Protein lin-54 homolog
5fd3 B 599 B 601
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 599 and 601.
Details
Redox score ?
84
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
7
% buried
42
Peptide accession
Q6MZP7
Residue number A
599
Residue number B
601
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 599 of Protein lin-54 homolog
Cysteine 601 of Protein lin-54 homolog
5fd3 A 525 A 551
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 525 and 551.
Details
Redox score ?
83
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
28
Peptide accession
Q6MZP7
Residue number A
525
Residue number B
551
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 525 of Protein lin-54 homolog
Cysteine 551 of Protein lin-54 homolog
5fd3 A 611 A 626
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 611 and 626.
Details
Redox score ?
83
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
56
Minimum pKa ?
2
% buried
34
Peptide accession
Q6MZP7
Residue number A
611
Residue number B
626
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 611 of Protein lin-54 homolog
Cysteine 626 of Protein lin-54 homolog
5fd3 A 537 A 546
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 537 and 546.
Details
Redox score ?
83
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
5
% buried
nan
Peptide accession
Q6MZP7
Residue number A
537
Residue number B
546
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 537 of Protein lin-54 homolog
Cysteine 546 of Protein lin-54 homolog
5fd3 B 549 B 551
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 549 and 551.
Details
Redox score ?
83
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
53
Minimum pKa ?
7
% buried
22
Peptide accession
Q6MZP7
Residue number A
549
Residue number B
551
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 549 of Protein lin-54 homolog
Cysteine 551 of Protein lin-54 homolog
5fd3 A 611 A 624
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 611 and 624.
Details
Redox score ?
82
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
53
Minimum pKa ?
2
% buried
28
Peptide accession
Q6MZP7
Residue number A
611
Residue number B
624
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 611 of Protein lin-54 homolog
Cysteine 624 of Protein lin-54 homolog
5fd3 B 599 B 606
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 599 and 606.
Details
Redox score ?
82
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
36
Peptide accession
Q6MZP7
Residue number A
599
Residue number B
606
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 599 of Protein lin-54 homolog
Cysteine 606 of Protein lin-54 homolog
5fd3 A 525 A 527
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 525 and 527.
Details
Redox score ?
80
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
48
Peptide accession
Q6MZP7
Residue number A
525
Residue number B
527
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 525 of Protein lin-54 homolog
Cysteine 527 of Protein lin-54 homolog
5fd3 B 599 B 613
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 599 and 613.
Details
Redox score ?
80
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
7
% buried
26
Peptide accession
Q6MZP7
Residue number A
599
Residue number B
613
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 599 of Protein lin-54 homolog
Cysteine 613 of Protein lin-54 homolog
5fd3 A 606 A 629
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 606 and 629.
Details
Redox score ?
78
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
8
% buried
32
Peptide accession
Q6MZP7
Residue number A
606
Residue number B
629
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 606 of Protein lin-54 homolog
Cysteine 629 of Protein lin-54 homolog
5fd3 B 525 B 532
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 525 and 532.
Details
Redox score ?
78
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
8
% buried
46
Peptide accession
Q6MZP7
Residue number A
525
Residue number B
532
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 525 of Protein lin-54 homolog
Cysteine 532 of Protein lin-54 homolog
5fd3 A 525 A 539
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 525 and 539.
Details
Redox score ?
77
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
34
Peptide accession
Q6MZP7
Residue number A
525
Residue number B
539
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 525 of Protein lin-54 homolog
Cysteine 539 of Protein lin-54 homolog
5fd3 A 525 A 537
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 525 and 537.
Details
Redox score ?
77
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
nan
Peptide accession
Q6MZP7
Residue number A
525
Residue number B
537
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 525 of Protein lin-54 homolog
Cysteine 537 of Protein lin-54 homolog
5fd3 A 611 A 629
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 611 and 629.
Details
Redox score ?
77
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
2
% buried
36
Peptide accession
Q6MZP7
Residue number A
611
Residue number B
629
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 611 of Protein lin-54 homolog
Cysteine 629 of Protein lin-54 homolog
5fd3 A 606 A 626
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 606 and 626.
Details
Redox score ?
77
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
30
Peptide accession
Q6MZP7
Residue number A
606
Residue number B
626
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 606 of Protein lin-54 homolog
Cysteine 626 of Protein lin-54 homolog
5fd3 B 532 B 551
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 532 and 551.
Details
Redox score ?
77
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
42
Peptide accession
Q6MZP7
Residue number A
532
Residue number B
551
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 532 of Protein lin-54 homolog
Cysteine 551 of Protein lin-54 homolog
5fd3 B 532 B 554
A redox-regulated disulphide may form within Protein lin-54 homolog between cysteines 532 and 554.
Details
Redox score ?
76
PDB code
5fd3
Structure name
structure of lin54 tesmin domain bound to dna
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
8
% buried
46
Peptide accession
Q6MZP7
Residue number A
532
Residue number B
554
Peptide name
Protein lin-54 homolog
Ligandability
Cysteine 532 of Protein lin-54 homolog
Cysteine 554 of Protein lin-54 homolog
If this tool was useful for finding a disulphide, please cite: