E3 ubiquitin-protein ligase RNF216
Intramolecular
Cysteine 714 and cysteine 724
Cysteine 530 and cysteine 564
Cysteine 724 and cysteine 727
Cysteine 714 and cysteine 727
Cysteine 623 and cysteine 628
Cysteine 678 and cysteine 693
Cysteine 608 and cysteine 628
Cysteine 675 and cysteine 678
Cysteine 675 and cysteine 695
Cysteine 633 and cysteine 636
More...Cysteine 633 and cysteine 648
Cysteine 530 and cysteine 559
Cysteine 605 and cysteine 628
Cysteine 636 and cysteine 648
Cysteine 693 and cysteine 695
Cysteine 608 and cysteine 623
Cysteine 675 and cysteine 693
Cysteine 515 and cysteine 518
Cysteine 703 and cysteine 730
Cysteine 518 and cysteine 540
Cysteine 518 and cysteine 537
Cysteine 559 and cysteine 564
Cysteine 564 and cysteine 566
Cysteine 700 and cysteine 703
Cysteine 605 and cysteine 623
Cysteine 517 and cysteine 540
Cysteine 605 and cysteine 608
Cysteine 530 and cysteine 566
Cysteine 700 and cysteine 730
Cysteine 515 and cysteine 517
Cysteine 678 and cysteine 695
Cysteine 517 and cysteine 518
Cysteine 515 and cysteine 537
Cysteine 537 and cysteine 540
Cysteine 517 and cysteine 537
Cysteine 559 and cysteine 566
Cysteine 714 and cysteine 730
Cysteine 727 and cysteine 730
Cysteine 688 and cysteine 700
Cysteine 515 and cysteine 540
8eb0 A 714 A 724
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 714 and 724.
Details
Redox score ?
95
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
44
Minimum pKa ?
6
% buried
4
Peptide accession
Q9NWF9
Residue number A
714
Residue number B
724
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 714 of E3 ubiquitin-protein ligase RNF216
Cysteine 724 of E3 ubiquitin-protein ligase RNF216
8eb0 A 530 A 564
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 530 and 564.
Details
Redox score ?
91
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
10
Peptide accession
Q9NWF9
Residue number A
530
Residue number B
564
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 530 of E3 ubiquitin-protein ligase RNF216
Cysteine 564 of E3 ubiquitin-protein ligase RNF216
7m4m A 724 A 727
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 724 and 727.
Details
Redox score ?
91
PDB code
7m4m
Structure name
crystal structure of rbr e3 ligase rnf216 with ubiquitin
Structure deposition date
2021-03-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
38
Minimum pKa ?
7
% buried
0
Peptide accession
Q9NWF9
Residue number A
724
Residue number B
727
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 724 of E3 ubiquitin-protein ligase RNF216
Cysteine 727 of E3 ubiquitin-protein ligase RNF216
7m4m B 714 B 727
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 714 and 727.
Details
Redox score ?
90
PDB code
7m4m
Structure name
crystal structure of rbr e3 ligase rnf216 with ubiquitin
Structure deposition date
2021-03-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
42
Minimum pKa ?
6
% buried
3
Peptide accession
Q9NWF9
Residue number A
714
Residue number B
727
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 714 of E3 ubiquitin-protein ligase RNF216
Cysteine 727 of E3 ubiquitin-protein ligase RNF216
8eb0 A 623 A 628
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 623 and 628.
Details
Redox score ?
88
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
19
Peptide accession
Q9NWF9
Residue number A
623
Residue number B
628
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 623 of E3 ubiquitin-protein ligase RNF216
Cysteine 628 of E3 ubiquitin-protein ligase RNF216
7m4m B 678 B 693
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 678 and 693.
Details
Redox score ?
88
PDB code
7m4m
Structure name
crystal structure of rbr e3 ligase rnf216 with ubiquitin
Structure deposition date
2021-03-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
5
% buried
13
Peptide accession
Q9NWF9
Residue number A
678
Residue number B
693
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 678 of E3 ubiquitin-protein ligase RNF216
Cysteine 693 of E3 ubiquitin-protein ligase RNF216
8eb0 A 608 A 628
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 608 and 628.
Details
Redox score ?
88
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
46
Minimum pKa ?
6
% buried
18
Peptide accession
Q9NWF9
Residue number A
608
Residue number B
628
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 608 of E3 ubiquitin-protein ligase RNF216
Cysteine 628 of E3 ubiquitin-protein ligase RNF216
7m4m A 675 A 678
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 675 and 678.
Details
Redox score ?
87
PDB code
7m4m
Structure name
crystal structure of rbr e3 ligase rnf216 with ubiquitin
Structure deposition date
2021-03-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
11
Peptide accession
Q9NWF9
Residue number A
675
Residue number B
678
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 675 of E3 ubiquitin-protein ligase RNF216
Cysteine 678 of E3 ubiquitin-protein ligase RNF216
7m4m A 675 A 695
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 675 and 695.
Details
Redox score ?
87
PDB code
7m4m
Structure name
crystal structure of rbr e3 ligase rnf216 with ubiquitin
Structure deposition date
2021-03-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
50
Minimum pKa ?
7
% buried
8
Peptide accession
Q9NWF9
Residue number A
675
Residue number B
695
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 675 of E3 ubiquitin-protein ligase RNF216
Cysteine 695 of E3 ubiquitin-protein ligase RNF216
7m4m B 633 B 636
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 633 and 636.
Details
Redox score ?
85
PDB code
7m4m
Structure name
crystal structure of rbr e3 ligase rnf216 with ubiquitin
Structure deposition date
2021-03-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
5
% buried
6
Peptide accession
Q9NWF9
Residue number A
633
Residue number B
636
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 633 of E3 ubiquitin-protein ligase RNF216
Cysteine 636 of E3 ubiquitin-protein ligase RNF216
7m4m A 633 A 648
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 633 and 648.
Details
Redox score ?
85
PDB code
7m4m
Structure name
crystal structure of rbr e3 ligase rnf216 with ubiquitin
Structure deposition date
2021-03-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
5
% buried
4
Peptide accession
Q9NWF9
Residue number A
633
Residue number B
648
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 633 of E3 ubiquitin-protein ligase RNF216
Cysteine 648 of E3 ubiquitin-protein ligase RNF216
8eb0 A 530 A 559
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 530 and 559.
Details
Redox score ?
85
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
6
% buried
31
Peptide accession
Q9NWF9
Residue number A
530
Residue number B
559
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 530 of E3 ubiquitin-protein ligase RNF216
Cysteine 559 of E3 ubiquitin-protein ligase RNF216
8eb0 A 605 A 628
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 605 and 628.
Details
Redox score ?
84
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
26
Peptide accession
Q9NWF9
Residue number A
605
Residue number B
628
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 605 of E3 ubiquitin-protein ligase RNF216
Cysteine 628 of E3 ubiquitin-protein ligase RNF216
7m4m A 636 A 648
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 636 and 648.
Details
Redox score ?
84
PDB code
7m4m
Structure name
crystal structure of rbr e3 ligase rnf216 with ubiquitin
Structure deposition date
2021-03-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
0
Peptide accession
Q9NWF9
Residue number A
636
Residue number B
648
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 636 of E3 ubiquitin-protein ligase RNF216
Cysteine 648 of E3 ubiquitin-protein ligase RNF216
7m4m A 693 A 695
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 693 and 695.
Details
Redox score ?
82
PDB code
7m4m
Structure name
crystal structure of rbr e3 ligase rnf216 with ubiquitin
Structure deposition date
2021-03-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
11
Peptide accession
Q9NWF9
Residue number A
693
Residue number B
695
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 693 of E3 ubiquitin-protein ligase RNF216
Cysteine 695 of E3 ubiquitin-protein ligase RNF216
8eb0 A 608 A 623
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 608 and 623.
Details
Redox score ?
82
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
8
% buried
28
Peptide accession
Q9NWF9
Residue number A
608
Residue number B
623
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 608 of E3 ubiquitin-protein ligase RNF216
Cysteine 623 of E3 ubiquitin-protein ligase RNF216
7m4n B 675 B 693
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 675 and 693.
Details
Redox score ?
81
PDB code
7m4n
Structure name
crystal structure of rbr e3 ligase rnf216 in complex with k63-linked di-ubiquitin
Structure deposition date
2021-03-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
24
Peptide accession
Q9NWF9
Residue number A
675
Residue number B
693
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 675 of E3 ubiquitin-protein ligase RNF216
Cysteine 693 of E3 ubiquitin-protein ligase RNF216
8eb0 A 515 A 518
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 515 and 518.
Details
Redox score ?
81
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
6
% buried
nan
Peptide accession
Q9NWF9
Residue number A
515
Residue number B
518
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 515 of E3 ubiquitin-protein ligase RNF216
Cysteine 518 of E3 ubiquitin-protein ligase RNF216
7m4m B 703 B 730
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 703 and 730.
Details
Redox score ?
81
PDB code
7m4m
Structure name
crystal structure of rbr e3 ligase rnf216 with ubiquitin
Structure deposition date
2021-03-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
26
Peptide accession
Q9NWF9
Residue number A
703
Residue number B
730
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 703 of E3 ubiquitin-protein ligase RNF216
Cysteine 730 of E3 ubiquitin-protein ligase RNF216
8eb0 A 518 A 540
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 518 and 540.
Details
Redox score ?
79
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
78
Minimum pKa ?
6
% buried
72
Peptide accession
Q9NWF9
Residue number A
518
Residue number B
540
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 518 of E3 ubiquitin-protein ligase RNF216
Cysteine 540 of E3 ubiquitin-protein ligase RNF216
8eb0 A 518 A 537
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 518 and 537.
Details
Redox score ?
79
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
6
% buried
61
Peptide accession
Q9NWF9
Residue number A
518
Residue number B
537
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 518 of E3 ubiquitin-protein ligase RNF216
Cysteine 537 of E3 ubiquitin-protein ligase RNF216
8eb0 A 559 A 564
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 559 and 564.
Details
Redox score ?
78
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
22
Peptide accession
Q9NWF9
Residue number A
559
Residue number B
564
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 559 of E3 ubiquitin-protein ligase RNF216
Cysteine 564 of E3 ubiquitin-protein ligase RNF216
8eb0 A 564 A 566
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 564 and 566.
Details
Redox score ?
76
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
41
Minimum pKa ?
10
% buried
0
Peptide accession
Q9NWF9
Residue number A
564
Residue number B
566
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 564 of E3 ubiquitin-protein ligase RNF216
Cysteine 566 of E3 ubiquitin-protein ligase RNF216
8eb0 A 700 A 703
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 700 and 703.
Details
Redox score ?
76
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
7
% buried
36
Peptide accession
Q9NWF9
Residue number A
700
Residue number B
703
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 700 of E3 ubiquitin-protein ligase RNF216
Cysteine 703 of E3 ubiquitin-protein ligase RNF216
8eb0 A 605 A 623
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 605 and 623.
Details
Redox score ?
74
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
8
% buried
36
Peptide accession
Q9NWF9
Residue number A
605
Residue number B
623
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 605 of E3 ubiquitin-protein ligase RNF216
Cysteine 623 of E3 ubiquitin-protein ligase RNF216
8eb0 A 517 A 540
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 517 and 540.
Details
Redox score ?
74
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
7
% buried
94
Peptide accession
Q9NWF9
Residue number A
517
Residue number B
540
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 517 of E3 ubiquitin-protein ligase RNF216
Cysteine 540 of E3 ubiquitin-protein ligase RNF216
8eb0 A 605 A 608
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 605 and 608.
Details
Redox score ?
72
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
35
Peptide accession
Q9NWF9
Residue number A
605
Residue number B
608
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 605 of E3 ubiquitin-protein ligase RNF216
Cysteine 608 of E3 ubiquitin-protein ligase RNF216
8eb0 A 530 A 566
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 530 and 566.
Details
Redox score ?
72
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
47
Minimum pKa ?
6
% buried
10
Peptide accession
Q9NWF9
Residue number A
530
Residue number B
566
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 530 of E3 ubiquitin-protein ligase RNF216
Cysteine 566 of E3 ubiquitin-protein ligase RNF216
7m4m B 700 B 730
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 700 and 730.
Details
Redox score ?
71
PDB code
7m4m
Structure name
crystal structure of rbr e3 ligase rnf216 with ubiquitin
Structure deposition date
2021-03-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
9
% buried
38
Peptide accession
Q9NWF9
Residue number A
700
Residue number B
730
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 700 of E3 ubiquitin-protein ligase RNF216
Cysteine 730 of E3 ubiquitin-protein ligase RNF216
8eb0 A 515 A 517
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 515 and 517.
Details
Redox score ?
70
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
nan
Peptide accession
Q9NWF9
Residue number A
515
Residue number B
517
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 515 of E3 ubiquitin-protein ligase RNF216
Cysteine 517 of E3 ubiquitin-protein ligase RNF216
8eb0 A 678 A 695
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 678 and 695.
Details
Redox score ?
64
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
14
% buried
nan
Peptide accession
Q9NWF9
Residue number A
678
Residue number B
695
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 678 of E3 ubiquitin-protein ligase RNF216
Cysteine 695 of E3 ubiquitin-protein ligase RNF216
8eb0 A 517 A 518
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 517 and 518.
Details
Redox score ?
63
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
78
Minimum pKa ?
6
% buried
78
Peptide accession
Q9NWF9
Residue number A
517
Residue number B
518
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 517 of E3 ubiquitin-protein ligase RNF216
Cysteine 518 of E3 ubiquitin-protein ligase RNF216
8eb0 A 515 A 537
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 515 and 537.
Details
Redox score ?
62
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
15
% buried
nan
Peptide accession
Q9NWF9
Residue number A
515
Residue number B
537
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 515 of E3 ubiquitin-protein ligase RNF216
Cysteine 537 of E3 ubiquitin-protein ligase RNF216
8eb0 A 537 A 540
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 537 and 540.
Details
Redox score ?
61
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
73
Minimum pKa ?
15
% buried
78
Peptide accession
Q9NWF9
Residue number A
537
Residue number B
540
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 537 of E3 ubiquitin-protein ligase RNF216
Cysteine 540 of E3 ubiquitin-protein ligase RNF216
8eb0 A 517 A 537
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 517 and 537. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
7
% buried
84
Peptide accession
Q9NWF9
Residue number A
517
Residue number B
537
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 517 of E3 ubiquitin-protein ligase RNF216
Cysteine 537 of E3 ubiquitin-protein ligase RNF216
8eb0 A 559 A 566
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 559 and 566. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
22
Peptide accession
Q9NWF9
Residue number A
559
Residue number B
566
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 559 of E3 ubiquitin-protein ligase RNF216
Cysteine 566 of E3 ubiquitin-protein ligase RNF216
7m4m A 714 A 730
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 714 and 730. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
7m4m
Structure name
crystal structure of rbr e3 ligase rnf216 with ubiquitin
Structure deposition date
2021-03-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
21
Peptide accession
Q9NWF9
Residue number A
714
Residue number B
730
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 714 of E3 ubiquitin-protein ligase RNF216
Cysteine 730 of E3 ubiquitin-protein ligase RNF216
8eb0 A 727 A 730
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 727 and 730. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
10
Peptide accession
Q9NWF9
Residue number A
727
Residue number B
730
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 727 of E3 ubiquitin-protein ligase RNF216
Cysteine 730 of E3 ubiquitin-protein ligase RNF216
7m4m B 688 B 700
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 688 and 700. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
7m4m
Structure name
crystal structure of rbr e3 ligase rnf216 with ubiquitin
Structure deposition date
2021-03-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
9
% buried
35
Peptide accession
Q9NWF9
Residue number A
688
Residue number B
700
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 688 of E3 ubiquitin-protein ligase RNF216
Cysteine 700 of E3 ubiquitin-protein ligase RNF216
8eb0 A 515 A 540
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF216 between cysteines 515 and 540. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
8eb0
Structure name
rnf216/e2-ub/ub transthiolation complex
Structure deposition date
2022-08-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
29
% buried
nan
Peptide accession
Q9NWF9
Residue number A
515
Residue number B
540
Peptide name
E3 ubiquitin-protein ligase RNF216
Ligandability
Cysteine 515 of E3 ubiquitin-protein ligase RNF216
Cysteine 540 of E3 ubiquitin-protein ligase RNF216
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