Tudor domain-containing protein 1
Intramolecular
Cysteine 531 and cysteine 591
Cysteine 747 and cysteine 764
Cysteine 511 and cysteine 607
Cysteine 531 and cysteine 549
Cysteine 725 and cysteine 822
Cysteine 549 and cysteine 591
Cysteine 715 and cysteine 725
Cysteine 548 and cysteine 549
Cysteine 747 and cysteine 763
Cysteine 715 and cysteine 822
More...Cysteine 763 and cysteine 764
Cysteine 548 and cysteine 591
Cysteine 531 and cysteine 548
5m9n A 530 A 590
A redox-regulated disulphide may form within Tudor domain-containing protein 1 between cysteines 531 and 591 (530 and 590 respectively in this structure).
Details
Redox score ?
81
PDB code
5m9n
Structure name
crystal structure of human tdrd1 extended tudor domain in complex with a symmetrically dimethylated e2f peptide
Structure deposition date
2016-11-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BXT4
Residue number A
531
Residue number B
591
Peptide name
Tudor domain-containing protein 1
Ligandability
Cysteine 531 of Tudor domain-containing protein 1
Cysteine 591 of Tudor domain-containing protein 1
4b9x A 747 A 764
A redox-regulated disulphide may form within Tudor domain-containing protein 1 between cysteines 747 and 764.
Details
Redox score ?
75
PDB code
4b9x
Structure name
structure of extended tudor domain td3 from mouse tdrd1
Structure deposition date
2012-09-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
8
% buried
64
Peptide accession
Q99MV1
Residue number A
747
Residue number B
764
Peptide name
Tudor domain-containing protein 1
Ligandability
Cysteine 747 of Tudor domain-containing protein 1
Cysteine 764 of Tudor domain-containing protein 1
5m9n A 510 A 606
A redox-regulated disulphide may form within Tudor domain-containing protein 1 between cysteines 511 and 607 (510 and 606 respectively in this structure).
Details
Redox score ?
70
PDB code
5m9n
Structure name
crystal structure of human tdrd1 extended tudor domain in complex with a symmetrically dimethylated e2f peptide
Structure deposition date
2016-11-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
8
% buried
96
Peptide accession
Q9BXT4
Residue number A
511
Residue number B
607
Peptide name
Tudor domain-containing protein 1
Ligandability
Cysteine 511 of Tudor domain-containing protein 1
Cysteine 607 of Tudor domain-containing protein 1
5m9n B 530 B 548
A redox-regulated disulphide may form within Tudor domain-containing protein 1 between cysteines 531 and 549 (530 and 548 respectively in this structure).
Details
Redox score ?
68
PDB code
5m9n
Structure name
crystal structure of human tdrd1 extended tudor domain in complex with a symmetrically dimethylated e2f peptide
Structure deposition date
2016-11-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
nan
Peptide accession
Q9BXT4
Residue number A
531
Residue number B
549
Peptide name
Tudor domain-containing protein 1
Ligandability
Cysteine 531 of Tudor domain-containing protein 1
Cysteine 549 of Tudor domain-containing protein 1
4b9w A 725 A 822
A redox-regulated disulphide may form within Tudor domain-containing protein 1 between cysteines 725 and 822.
Details
Redox score ?
67
PDB code
4b9w
Structure name
structure of extended tudor domain td3 from mouse tdrd1 in complex with mili peptide containing dimethylarginine 45
Structure deposition date
2012-09-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
85
Minimum pKa ?
10
% buried
100
Peptide accession
Q99MV1
Residue number A
725
Residue number B
822
Peptide name
Tudor domain-containing protein 1
Ligandability
Cysteine 725 of Tudor domain-containing protein 1
Cysteine 822 of Tudor domain-containing protein 1
5m9n A 548 A 590
A redox-regulated disulphide may form within Tudor domain-containing protein 1 between cysteines 549 and 591 (548 and 590 respectively in this structure).
Details
Redox score ?
61
PDB code
5m9n
Structure name
crystal structure of human tdrd1 extended tudor domain in complex with a symmetrically dimethylated e2f peptide
Structure deposition date
2016-11-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
13
% buried
nan
Peptide accession
Q9BXT4
Residue number A
549
Residue number B
591
Peptide name
Tudor domain-containing protein 1
Ligandability
Cysteine 549 of Tudor domain-containing protein 1
Cysteine 591 of Tudor domain-containing protein 1
4b9x A 715 A 725
A redox-regulated disulphide may form within Tudor domain-containing protein 1 between cysteines 715 and 725. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
4b9x
Structure name
structure of extended tudor domain td3 from mouse tdrd1
Structure deposition date
2012-09-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
88
Peptide accession
Q99MV1
Residue number A
715
Residue number B
725
Peptide name
Tudor domain-containing protein 1
Ligandability
Cysteine 715 of Tudor domain-containing protein 1
Cysteine 725 of Tudor domain-containing protein 1
5m9n A 547 A 548
A redox-regulated disulphide may form within Tudor domain-containing protein 1 between cysteines 548 and 549 (547 and 548 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
5m9n
Structure name
crystal structure of human tdrd1 extended tudor domain in complex with a symmetrically dimethylated e2f peptide
Structure deposition date
2016-11-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
13
% buried
100
Peptide accession
Q9BXT4
Residue number A
548
Residue number B
549
Peptide name
Tudor domain-containing protein 1
Ligandability
Cysteine 548 of Tudor domain-containing protein 1
Cysteine 549 of Tudor domain-containing protein 1
4b9x A 747 A 763
A redox-regulated disulphide may form within Tudor domain-containing protein 1 between cysteines 747 and 763. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
4b9x
Structure name
structure of extended tudor domain td3 from mouse tdrd1
Structure deposition date
2012-09-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
8
% buried
68
Peptide accession
Q99MV1
Residue number A
747
Residue number B
763
Peptide name
Tudor domain-containing protein 1
Ligandability
Cysteine 747 of Tudor domain-containing protein 1
Cysteine 763 of Tudor domain-containing protein 1
4b9x A 715 A 822
A redox-regulated disulphide may form within Tudor domain-containing protein 1 between cysteines 715 and 822. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
4b9x
Structure name
structure of extended tudor domain td3 from mouse tdrd1
Structure deposition date
2012-09-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
88
Peptide accession
Q99MV1
Residue number A
715
Residue number B
822
Peptide name
Tudor domain-containing protein 1
Ligandability
Cysteine 715 of Tudor domain-containing protein 1
Cysteine 822 of Tudor domain-containing protein 1
4b9w A 763 A 764
A redox-regulated disulphide may form within Tudor domain-containing protein 1 between cysteines 763 and 764. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
4b9w
Structure name
structure of extended tudor domain td3 from mouse tdrd1 in complex with mili peptide containing dimethylarginine 45
Structure deposition date
2012-09-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
86
Minimum pKa ?
13
% buried
94
Peptide accession
Q99MV1
Residue number A
763
Residue number B
764
Peptide name
Tudor domain-containing protein 1
Ligandability
Cysteine 763 of Tudor domain-containing protein 1
Cysteine 764 of Tudor domain-containing protein 1
5m9n A 547 A 590
A redox-regulated disulphide may form within Tudor domain-containing protein 1 between cysteines 548 and 591 (547 and 590 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
5m9n
Structure name
crystal structure of human tdrd1 extended tudor domain in complex with a symmetrically dimethylated e2f peptide
Structure deposition date
2016-11-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
nan
Peptide accession
Q9BXT4
Residue number A
548
Residue number B
591
Peptide name
Tudor domain-containing protein 1
Ligandability
Cysteine 548 of Tudor domain-containing protein 1
Cysteine 591 of Tudor domain-containing protein 1
5m9n B 530 B 547
A redox-regulated disulphide may form within Tudor domain-containing protein 1 between cysteines 531 and 548 (530 and 547 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
5m9n
Structure name
crystal structure of human tdrd1 extended tudor domain in complex with a symmetrically dimethylated e2f peptide
Structure deposition date
2016-11-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
13
% buried
nan
Peptide accession
Q9BXT4
Residue number A
531
Residue number B
548
Peptide name
Tudor domain-containing protein 1
Ligandability
Cysteine 531 of Tudor domain-containing protein 1
Cysteine 548 of Tudor domain-containing protein 1
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