E3 ubiquitin-protein ligase RNF126
Intramolecular
Cysteine 29 and cysteine 32
Cysteine 249 and cysteine 268
Cysteine 231 and cysteine 234
Cysteine 268 and cysteine 271
Cysteine 16 and cysteine 32
Cysteine 13 and cysteine 16
Cysteine 231 and cysteine 257
Cysteine 13 and cysteine 32
Cysteine 249 and cysteine 271
Cysteine 16 and cysteine 29
More...Cysteine 13 and cysteine 29
Cysteine 15 and cysteine 32
Cysteine 234 and cysteine 257
Cysteine 13 and cysteine 15
Cysteine 15 and cysteine 16
Cysteine 15 and cysteine 29
2n9o A 29 A 32
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF126 between cysteines 29 and 32.
Details
Redox score ?
87
PDB code
2n9o
Structure name
solution structure of rnf126 n-terminal zinc finger domain
Structure deposition date
2015-12-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
6
% buried
0
Peptide accession
Q9BV68
Residue number A
29
Residue number B
32
Peptide name
E3 ubiquitin-protein ligase RNF126
Ligandability
Cysteine 29 of E3 ubiquitin-protein ligase RNF126
Cysteine 32 of E3 ubiquitin-protein ligase RNF126
2ect A 36 A 55
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF126 between cysteines 249 and 268 (36 and 55 respectively in this structure).
Details
Redox score ?
86
PDB code
2ect
Structure name
solution structure of the zinc finger, c3hc4 type (ring finger) domain of ring finger protein 126
Structure deposition date
2007-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
8
Peptide accession
Q91YL2
Residue number A
249
Residue number B
268
Peptide name
E3 ubiquitin-protein ligase RNF126
Ligandability
Cysteine 249 of E3 ubiquitin-protein ligase RNF126
Cysteine 268 of E3 ubiquitin-protein ligase RNF126
2ect A 18 A 21
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF126 between cysteines 231 and 234 (18 and 21 respectively in this structure).
Details
Redox score ?
86
PDB code
2ect
Structure name
solution structure of the zinc finger, c3hc4 type (ring finger) domain of ring finger protein 126
Structure deposition date
2007-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
10
Peptide accession
Q91YL2
Residue number A
231
Residue number B
234
Peptide name
E3 ubiquitin-protein ligase RNF126
Ligandability
Cysteine 231 of E3 ubiquitin-protein ligase RNF126
Cysteine 234 of E3 ubiquitin-protein ligase RNF126
2ect A 55 A 58
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF126 between cysteines 268 and 271 (55 and 58 respectively in this structure).
Details
Redox score ?
84
PDB code
2ect
Structure name
solution structure of the zinc finger, c3hc4 type (ring finger) domain of ring finger protein 126
Structure deposition date
2007-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
7
% buried
7
Peptide accession
Q91YL2
Residue number A
268
Residue number B
271
Peptide name
E3 ubiquitin-protein ligase RNF126
Ligandability
Cysteine 268 of E3 ubiquitin-protein ligase RNF126
Cysteine 271 of E3 ubiquitin-protein ligase RNF126
2n9p A 16 A 32
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF126 between cysteines 16 and 32.
Details
Redox score ?
83
PDB code
2n9p
Structure name
solution structure of rnf126 n-terminal zinc finger domain in complex with bag6 ubiquitin-like domain
Structure deposition date
2015-12-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
6
% buried
6
Peptide accession
Q9BV68
Residue number A
16
Residue number B
32
Peptide name
E3 ubiquitin-protein ligase RNF126
Ligandability
Cysteine 16 of E3 ubiquitin-protein ligase RNF126
Cysteine 32 of E3 ubiquitin-protein ligase RNF126
2n9o A 13 A 16
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF126 between cysteines 13 and 16.
Details
Redox score ?
83
PDB code
2n9o
Structure name
solution structure of rnf126 n-terminal zinc finger domain
Structure deposition date
2015-12-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
7
% buried
0
Peptide accession
Q9BV68
Residue number A
13
Residue number B
16
Peptide name
E3 ubiquitin-protein ligase RNF126
Ligandability
Cysteine 13 of E3 ubiquitin-protein ligase RNF126
Cysteine 16 of E3 ubiquitin-protein ligase RNF126
2ect A 18 A 44
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF126 between cysteines 231 and 257 (18 and 44 respectively in this structure).
Details
Redox score ?
83
PDB code
2ect
Structure name
solution structure of the zinc finger, c3hc4 type (ring finger) domain of ring finger protein 126
Structure deposition date
2007-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
12
Peptide accession
Q91YL2
Residue number A
231
Residue number B
257
Peptide name
E3 ubiquitin-protein ligase RNF126
Ligandability
Cysteine 231 of E3 ubiquitin-protein ligase RNF126
Cysteine 257 of E3 ubiquitin-protein ligase RNF126
2n9o A 13 A 32
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF126 between cysteines 13 and 32.
Details
Redox score ?
83
PDB code
2n9o
Structure name
solution structure of rnf126 n-terminal zinc finger domain
Structure deposition date
2015-12-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
7
% buried
0
Peptide accession
Q9BV68
Residue number A
13
Residue number B
32
Peptide name
E3 ubiquitin-protein ligase RNF126
Ligandability
Cysteine 13 of E3 ubiquitin-protein ligase RNF126
Cysteine 32 of E3 ubiquitin-protein ligase RNF126
2ect A 36 A 58
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF126 between cysteines 249 and 271 (36 and 58 respectively in this structure).
Details
Redox score ?
82
PDB code
2ect
Structure name
solution structure of the zinc finger, c3hc4 type (ring finger) domain of ring finger protein 126
Structure deposition date
2007-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
34
Minimum pKa ?
9
% buried
1
Peptide accession
Q91YL2
Residue number A
249
Residue number B
271
Peptide name
E3 ubiquitin-protein ligase RNF126
Ligandability
Cysteine 249 of E3 ubiquitin-protein ligase RNF126
Cysteine 271 of E3 ubiquitin-protein ligase RNF126
2n9p A 16 A 29
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF126 between cysteines 16 and 29.
Details
Redox score ?
81
PDB code
2n9p
Structure name
solution structure of rnf126 n-terminal zinc finger domain in complex with bag6 ubiquitin-like domain
Structure deposition date
2015-12-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
8
Peptide accession
Q9BV68
Residue number A
16
Residue number B
29
Peptide name
E3 ubiquitin-protein ligase RNF126
Ligandability
Cysteine 16 of E3 ubiquitin-protein ligase RNF126
Cysteine 29 of E3 ubiquitin-protein ligase RNF126
2n9p A 13 A 29
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF126 between cysteines 13 and 29.
Details
Redox score ?
79
PDB code
2n9p
Structure name
solution structure of rnf126 n-terminal zinc finger domain in complex with bag6 ubiquitin-like domain
Structure deposition date
2015-12-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
25
Peptide accession
Q9BV68
Residue number A
13
Residue number B
29
Peptide name
E3 ubiquitin-protein ligase RNF126
Ligandability
Cysteine 13 of E3 ubiquitin-protein ligase RNF126
Cysteine 29 of E3 ubiquitin-protein ligase RNF126
2n9o A 15 A 32
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF126 between cysteines 15 and 32.
Details
Redox score ?
78
PDB code
2n9o
Structure name
solution structure of rnf126 n-terminal zinc finger domain
Structure deposition date
2015-12-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
8
% buried
0
Peptide accession
Q9BV68
Residue number A
15
Residue number B
32
Peptide name
E3 ubiquitin-protein ligase RNF126
Ligandability
Cysteine 15 of E3 ubiquitin-protein ligase RNF126
Cysteine 32 of E3 ubiquitin-protein ligase RNF126
2ect A 21 A 44
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF126 between cysteines 234 and 257 (21 and 44 respectively in this structure).
Details
Redox score ?
75
PDB code
2ect
Structure name
solution structure of the zinc finger, c3hc4 type (ring finger) domain of ring finger protein 126
Structure deposition date
2007-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
3
Peptide accession
Q91YL2
Residue number A
234
Residue number B
257
Peptide name
E3 ubiquitin-protein ligase RNF126
Ligandability
Cysteine 234 of E3 ubiquitin-protein ligase RNF126
Cysteine 257 of E3 ubiquitin-protein ligase RNF126
2n9o A 13 A 15
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF126 between cysteines 13 and 15.
Details
Redox score ?
75
PDB code
2n9o
Structure name
solution structure of rnf126 n-terminal zinc finger domain
Structure deposition date
2015-12-01
Thiol separation (Å)
5
Half-sphere exposure sum ?
46
Minimum pKa ?
7
% buried
0
Peptide accession
Q9BV68
Residue number A
13
Residue number B
15
Peptide name
E3 ubiquitin-protein ligase RNF126
Ligandability
Cysteine 13 of E3 ubiquitin-protein ligase RNF126
Cysteine 15 of E3 ubiquitin-protein ligase RNF126
2n9o A 15 A 16
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF126 between cysteines 15 and 16.
Details
Redox score ?
72
PDB code
2n9o
Structure name
solution structure of rnf126 n-terminal zinc finger domain
Structure deposition date
2015-12-01
Thiol separation (Å)
5
Half-sphere exposure sum ?
40
Minimum pKa ?
8
% buried
0
Peptide accession
Q9BV68
Residue number A
15
Residue number B
16
Peptide name
E3 ubiquitin-protein ligase RNF126
Ligandability
Cysteine 15 of E3 ubiquitin-protein ligase RNF126
Cysteine 16 of E3 ubiquitin-protein ligase RNF126
2n9o A 15 A 29
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF126 between cysteines 15 and 29.
Details
Redox score ?
67
PDB code
2n9o
Structure name
solution structure of rnf126 n-terminal zinc finger domain
Structure deposition date
2015-12-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
50
Minimum pKa ?
6
% buried
0
Peptide accession
Q9BV68
Residue number A
15
Residue number B
29
Peptide name
E3 ubiquitin-protein ligase RNF126
Ligandability
Cysteine 15 of E3 ubiquitin-protein ligase RNF126
Cysteine 29 of E3 ubiquitin-protein ligase RNF126
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