E3 ubiquitin-protein ligase RBX1
Intramolecular
Cysteine 53 and cysteine 68
Cysteine 42 and cysteine 45
Cysteine 53 and cysteine 56
Cysteine 75 and cysteine 94 L
Cysteine 45 and cysteine 83
Cysteine 56 and cysteine 68
Cysteine 42 and cysteine 83
Cysteine 45 and cysteine 53
Cysteine 42 and cysteine 53
Cysteine 42 and cysteine 94 L
More...Cysteine 42 and cysteine 68
Cysteine 56 and cysteine 83
Cysteine 68 and cysteine 83
Cysteine 45 and cysteine 68
Cysteine 42 and cysteine 56
Cysteine 53 and cysteine 83
Cysteine 45 and cysteine 56
1u6g B 53 B 68
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RBX1 between cysteines 53 and 68.
Details
Redox score ?
97
PDB code
1u6g
Structure name
crystal structure of the cand1-cul1-roc1 complex
Structure deposition date
2004-07-29
Thiol separation (Å)
3
Half-sphere exposure sum ?
64
Minimum pKa ?
1
% buried
46
Peptide accession
P62877
Residue number A
53
Residue number B
68
Peptide name
E3 ubiquitin-protein ligase RBX1
Ligandability
Cysteine 53 of E3 ubiquitin-protein ligase RBX1
Cysteine 68 of E3 ubiquitin-protein ligase RBX1
1u6g B 42 B 45
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RBX1 between cysteines 42 and 45.
Details
Redox score ?
86
PDB code
1u6g
Structure name
crystal structure of the cand1-cul1-roc1 complex
Structure deposition date
2004-07-29
Thiol separation (Å)
3
Half-sphere exposure sum ?
58
Minimum pKa ?
6
% buried
nan
Peptide accession
P62877
Residue number A
42
Residue number B
45
Peptide name
E3 ubiquitin-protein ligase RBX1
Ligandability
Cysteine 42 of E3 ubiquitin-protein ligase RBX1
Cysteine 45 of E3 ubiquitin-protein ligase RBX1
1ldk C 1053 C 1056
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RBX1 between cysteines 53 and 56 (1053 and 1056 respectively in this structure).
Details
Redox score ?
86
PDB code
1ldk
Structure name
structure of the cul1-rbx1-skp1-f boxskp2 scf ubiquitin ligase complex
Structure deposition date
2002-04-08
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
7
% buried
26
Peptide accession
P62877
Residue number A
53
Residue number B
56
Peptide name
E3 ubiquitin-protein ligase RBX1
Ligandability
Cysteine 53 of E3 ubiquitin-protein ligase RBX1
Cysteine 56 of E3 ubiquitin-protein ligase RBX1
1ldj B 75 B 94
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RBX1 between cysteines 75 and 94.
Details
Redox score ?
85
PDB code
1ldj
Structure name
structure of the cul1-rbx1-skp1-f boxskp2 scf ubiquitin ligase complex
Structure deposition date
2002-04-08
Thiol separation (Å)
3
Half-sphere exposure sum ?
56
Minimum pKa ?
5
% buried
45
Peptide accession
P62877
Residue number A
75
Residue number B
94
Peptide name
E3 ubiquitin-protein ligase RBX1
Ligandability
Cysteine 75 of E3 ubiquitin-protein ligase RBX1
Cysteine 94 of E3 ubiquitin-protein ligase RBX1
4f52 B 45 B 83
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RBX1 between cysteines 45 and 83.
Details
Redox score ?
80
PDB code
4f52
Structure name
structure of a glomulin-rbx1-cul1 complex
Structure deposition date
2012-05-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
82
Minimum pKa ?
6
% buried
nan
Peptide accession
P62877
Residue number A
45
Residue number B
83
Peptide name
E3 ubiquitin-protein ligase RBX1
Ligandability
Cysteine 45 of E3 ubiquitin-protein ligase RBX1
Cysteine 83 of E3 ubiquitin-protein ligase RBX1
1u6g B 56 B 68
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RBX1 between cysteines 56 and 68.
Details
Redox score ?
78
PDB code
1u6g
Structure name
crystal structure of the cand1-cul1-roc1 complex
Structure deposition date
2004-07-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
40
Peptide accession
P62877
Residue number A
56
Residue number B
68
Peptide name
E3 ubiquitin-protein ligase RBX1
Ligandability
Cysteine 56 of E3 ubiquitin-protein ligase RBX1
Cysteine 68 of E3 ubiquitin-protein ligase RBX1
3dpl R 42 R 83
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RBX1 between cysteines 42 and 83.
Details
Redox score ?
75
PDB code
3dpl
Structure name
structural insights into nedd8 activation of cullin-ring ligases: conformational control of conjugation
Structure deposition date
2008-07-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P62877
Residue number A
42
Residue number B
83
Peptide name
E3 ubiquitin-protein ligase RBX1
Ligandability
Cysteine 42 of E3 ubiquitin-protein ligase RBX1
Cysteine 83 of E3 ubiquitin-protein ligase RBX1
4a0c F 45 F 53
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RBX1 between cysteines 45 and 53.
Details
Redox score ?
68
PDB code
4a0c
Structure name
structure of the cand1-cul4b-rbx1 complex
Structure deposition date
2011-09-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
51
Minimum pKa ?
11
% buried
30
Peptide accession
P62878
Residue number A
45
Residue number B
53
Peptide name
E3 ubiquitin-protein ligase RBX1
Ligandability
Cysteine 45 of E3 ubiquitin-protein ligase RBX1
Cysteine 53 of E3 ubiquitin-protein ligase RBX1
4a0c F 42 F 53
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RBX1 between cysteines 42 and 53.
Details
Redox score ?
62
PDB code
4a0c
Structure name
structure of the cand1-cul4b-rbx1 complex
Structure deposition date
2011-09-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
58
Minimum pKa ?
7
% buried
44
Peptide accession
P62878
Residue number A
42
Residue number B
53
Peptide name
E3 ubiquitin-protein ligase RBX1
Ligandability
Cysteine 42 of E3 ubiquitin-protein ligase RBX1
Cysteine 53 of E3 ubiquitin-protein ligase RBX1
3dqv Y 42 Y 94
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RBX1 between cysteines 42 and 94. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
3dqv
Structure name
structural insights into nedd8 activation of cullin-ring ligases: conformational control of conjugation
Structure deposition date
2008-07-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
27
Peptide accession
P62877
Residue number A
42
Residue number B
94
Peptide name
E3 ubiquitin-protein ligase RBX1
Ligandability
Cysteine 42 of E3 ubiquitin-protein ligase RBX1
Cysteine 94 of E3 ubiquitin-protein ligase RBX1
3rtr B 42 B 68
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RBX1 between cysteines 42 and 68. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
3rtr
Structure name
a ring e3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-ring ligases
Structure deposition date
2011-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
6
% buried
80
Peptide accession
P62877
Residue number A
42
Residue number B
68
Peptide name
E3 ubiquitin-protein ligase RBX1
Ligandability
Cysteine 42 of E3 ubiquitin-protein ligase RBX1
Cysteine 68 of E3 ubiquitin-protein ligase RBX1
1ldj B 56 B 83
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RBX1 between cysteines 56 and 83. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
1ldj
Structure name
structure of the cul1-rbx1-skp1-f boxskp2 scf ubiquitin ligase complex
Structure deposition date
2002-04-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
52
Peptide accession
P62877
Residue number A
56
Residue number B
83
Peptide name
E3 ubiquitin-protein ligase RBX1
Ligandability
Cysteine 56 of E3 ubiquitin-protein ligase RBX1
Cysteine 83 of E3 ubiquitin-protein ligase RBX1
5n4w R 68 R 83
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RBX1 between cysteines 68 and 83. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
5n4w
Structure name
crystal structure of the cul2-rbx1-elobc-vhl ubiquitin ligase complex
Structure deposition date
2017-02-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
48
Peptide accession
P62877
Residue number A
68
Residue number B
83
Peptide name
E3 ubiquitin-protein ligase RBX1
Ligandability
Cysteine 68 of E3 ubiquitin-protein ligase RBX1
Cysteine 83 of E3 ubiquitin-protein ligase RBX1
4a0c D 45 D 68
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RBX1 between cysteines 45 and 68. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
4a0c
Structure name
structure of the cand1-cul4b-rbx1 complex
Structure deposition date
2011-09-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
60
Peptide accession
P62878
Residue number A
45
Residue number B
68
Peptide name
E3 ubiquitin-protein ligase RBX1
Ligandability
Cysteine 45 of E3 ubiquitin-protein ligase RBX1
Cysteine 68 of E3 ubiquitin-protein ligase RBX1
2lgv A 42 A 56
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RBX1 between cysteines 42 and 56. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
2lgv
Structure name
rbx1
Structure deposition date
2011-08-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P62877
Residue number A
42
Residue number B
56
Peptide name
E3 ubiquitin-protein ligase RBX1
Ligandability
Cysteine 42 of E3 ubiquitin-protein ligase RBX1
Cysteine 56 of E3 ubiquitin-protein ligase RBX1
4a0c D 53 D 83
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RBX1 between cysteines 53 and 83. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
4a0c
Structure name
structure of the cand1-cul4b-rbx1 complex
Structure deposition date
2011-09-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
23
% buried
nan
Peptide accession
P62878
Residue number A
53
Residue number B
83
Peptide name
E3 ubiquitin-protein ligase RBX1
Ligandability
Cysteine 53 of E3 ubiquitin-protein ligase RBX1
Cysteine 83 of E3 ubiquitin-protein ligase RBX1
2hye D 45 D 56
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RBX1 between cysteines 45 and 56. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
2hye
Structure name
crystal structure of the ddb1-cul4a-rbx1-sv5v complex
Structure deposition date
2006-08-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
18
% buried
nan
Peptide accession
P62877
Residue number A
45
Residue number B
56
Peptide name
E3 ubiquitin-protein ligase RBX1
Ligandability
Cysteine 45 of E3 ubiquitin-protein ligase RBX1
Cysteine 56 of E3 ubiquitin-protein ligase RBX1
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