Ubiquitin-protein ligase E3A
Intramolecular
Cysteine 44 and cysteine 49
Cysteine 49 and cysteine 83
Cysteine 44 and cysteine 83
Cysteine 57 and cysteine 374
Cysteine 49 and cysteine 57
Cysteine 49 and cysteine 54
Cysteine 44 and cysteine 54
Cysteine 57 and cysteine 1139
Cysteine 54 and cysteine 83
Cysteine 57 and cysteine 627
More...Cysteine 439 and cysteine 843 L
Cysteine 54 and cysteine 57
Cysteine 44 and cysteine 57
Cysteine 57 and cysteine 83
Cysteine 627 and cysteine 843 L
Cysteine 439 and cysteine 1138
Cysteine 57 and cysteine 198
Cysteine 439 and cysteine 627
Cysteine 439 and cysteine 1139
Cysteine 843 and cysteine 1142 L
Cysteine 310 and cysteine 439
Cysteine 480 and cysteine 374
Cysteine 310 and cysteine 843 L
Cysteine 198 and cysteine 374
Cysteine 310 and cysteine 1138
Cysteine 480 and cysteine 1063
Cysteine 310 and cysteine 1142
Cysteine 1030 and cysteine 374
Cysteine 1138 and cysteine 843 L
Cysteine 1032 and cysteine 374
Cysteine 1030 and cysteine 480
Cysteine 1032 and cysteine 198
Cysteine 1030 and cysteine 1063
Cysteine 1063 and cysteine 374
6u19 B 44 B 49
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 44 and 49.
Details
Redox score ?
84
PDB code
6u19
Structure name
solution structure of the razul domain from 26s proteasome subunit hrpn10/s5a complexed with the azul domain from e3 ligase e6ap/ube3a
Structure deposition date
2019-08-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
6
% buried
0
Peptide accession
Q05086
Residue number A
44
Residue number B
49
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 44 of Ubiquitin-protein ligase E3A
Cysteine 49 of Ubiquitin-protein ligase E3A
6u19 B 49 B 83
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 49 and 83.
Details
Redox score ?
82
PDB code
6u19
Structure name
solution structure of the razul domain from 26s proteasome subunit hrpn10/s5a complexed with the azul domain from e3 ligase e6ap/ube3a
Structure deposition date
2019-08-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
0
Peptide accession
Q05086
Residue number A
49
Residue number B
83
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 49 of Ubiquitin-protein ligase E3A
Cysteine 83 of Ubiquitin-protein ligase E3A
6u19 B 44 B 83
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 44 and 83.
Details
Redox score ?
82
PDB code
6u19
Structure name
solution structure of the razul domain from 26s proteasome subunit hrpn10/s5a complexed with the azul domain from e3 ligase e6ap/ube3a
Structure deposition date
2019-08-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
6
% buried
0
Peptide accession
Q05086
Residue number A
44
Residue number B
83
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 44 of Ubiquitin-protein ligase E3A
Cysteine 83 of Ubiquitin-protein ligase E3A
6sjv A 1035 A 1068
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 57 and 374 (1035 and 1068 respectively in this structure).
Details
Redox score ?
82
PDB code
6sjv
Structure name
structure of hpv18 e6 oncoprotein in complex with mutant e6ap lxxll motif
Structure deposition date
2019-08-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
6
% buried
8
Peptide accession
Q05086
Residue number A
57
Residue number B
374
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 57 of Ubiquitin-protein ligase E3A
Cysteine 374 of Ubiquitin-protein ligase E3A
6u19 B 49 B 57
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 49 and 57.
Details
Redox score ?
81
PDB code
6u19
Structure name
solution structure of the razul domain from 26s proteasome subunit hrpn10/s5a complexed with the azul domain from e3 ligase e6ap/ube3a
Structure deposition date
2019-08-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
0
Peptide accession
Q05086
Residue number A
49
Residue number B
57
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 49 of Ubiquitin-protein ligase E3A
Cysteine 57 of Ubiquitin-protein ligase E3A
6u19 B 49 B 54
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 49 and 54.
Details
Redox score ?
79
PDB code
6u19
Structure name
solution structure of the razul domain from 26s proteasome subunit hrpn10/s5a complexed with the azul domain from e3 ligase e6ap/ube3a
Structure deposition date
2019-08-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
8
Peptide accession
Q05086
Residue number A
49
Residue number B
54
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 49 of Ubiquitin-protein ligase E3A
Cysteine 54 of Ubiquitin-protein ligase E3A
6u19 B 44 B 54
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 44 and 54.
Details
Redox score ?
78
PDB code
6u19
Structure name
solution structure of the razul domain from 26s proteasome subunit hrpn10/s5a complexed with the azul domain from e3 ligase e6ap/ube3a
Structure deposition date
2019-08-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
6
% buried
8
Peptide accession
Q05086
Residue number A
44
Residue number B
54
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 44 of Ubiquitin-protein ligase E3A
Cysteine 54 of Ubiquitin-protein ligase E3A
6slm A 1103 A 1139
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 57 and 1139 (1103 and 1139 respectively in this structure).
Details
Redox score ?
78
PDB code
6slm
Structure name
crystal structure of full-length hpv31 e6 oncoprotein in complex with lxxll peptide of ubiquitin ligase e6ap
Structure deposition date
2019-08-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
nan
Peptide accession
Q05086
Residue number A
57
Residue number B
1139
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 57 of Ubiquitin-protein ligase E3A
Cysteine 1139 of Ubiquitin-protein ligase E3A
Cysteine 1139 in protein B could not be asigned to a Uniprot residue.
6u19 B 54 B 83
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 54 and 83.
Details
Redox score ?
75
PDB code
6u19
Structure name
solution structure of the razul domain from 26s proteasome subunit hrpn10/s5a complexed with the azul domain from e3 ligase e6ap/ube3a
Structure deposition date
2019-08-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
8
Peptide accession
Q05086
Residue number A
54
Residue number B
83
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 54 of Ubiquitin-protein ligase E3A
Cysteine 83 of Ubiquitin-protein ligase E3A
6slm A 1103 A 1136
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 57 and 627 (1103 and 1136 respectively in this structure).
Details
Redox score ?
73
PDB code
6slm
Structure name
crystal structure of full-length hpv31 e6 oncoprotein in complex with lxxll peptide of ubiquitin ligase e6ap
Structure deposition date
2019-08-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
nan
Peptide accession
Q05086
Residue number A
57
Residue number B
627
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 57 of Ubiquitin-protein ligase E3A
Cysteine 627 of Ubiquitin-protein ligase E3A
Uncertain whether structure cysteine 1136 has been assigned to correct residue.
6sjv A 1108 A 1141
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 439 and 843 (1108 and 1141 respectively in this structure).
Details
Redox score ?
71
PDB code
6sjv
Structure name
structure of hpv18 e6 oncoprotein in complex with mutant e6ap lxxll motif
Structure deposition date
2019-08-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
11
% buried
43
Peptide accession
Q05086
Residue number A
439
Residue number B
843
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 439 of Ubiquitin-protein ligase E3A
Cysteine 843 of Ubiquitin-protein ligase E3A
6u19 B 54 B 57
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 54 and 57.
Details
Redox score ?
63
PDB code
6u19
Structure name
solution structure of the razul domain from 26s proteasome subunit hrpn10/s5a complexed with the azul domain from e3 ligase e6ap/ube3a
Structure deposition date
2019-08-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
8
% buried
8
Peptide accession
Q05086
Residue number A
54
Residue number B
57
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 54 of Ubiquitin-protein ligase E3A
Cysteine 57 of Ubiquitin-protein ligase E3A
6u19 B 44 B 57
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 44 and 57.
Details
Redox score ?
62
PDB code
6u19
Structure name
solution structure of the razul domain from 26s proteasome subunit hrpn10/s5a complexed with the azul domain from e3 ligase e6ap/ube3a
Structure deposition date
2019-08-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
0
Peptide accession
Q05086
Residue number A
44
Residue number B
57
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 44 of Ubiquitin-protein ligase E3A
Cysteine 57 of Ubiquitin-protein ligase E3A
6u19 B 57 B 83
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 57 and 83. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
6u19
Structure name
solution structure of the razul domain from 26s proteasome subunit hrpn10/s5a complexed with the azul domain from e3 ligase e6ap/ube3a
Structure deposition date
2019-08-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
0
Peptide accession
Q05086
Residue number A
57
Residue number B
83
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 57 of Ubiquitin-protein ligase E3A
Cysteine 83 of Ubiquitin-protein ligase E3A
1d5f A 604 A 820
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 627 and 843 (604 and 820 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
1d5f
Structure name
structure of e6ap: insights into ubiquitination pathway
Structure deposition date
1999-10-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
74
Peptide accession
Q05086
Residue number A
627
Residue number B
843
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 627 of Ubiquitin-protein ligase E3A
Cysteine 843 of Ubiquitin-protein ligase E3A
6sjv A 1108 A 1138
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 439 and 1138 (1108 and 1138 respectively in this structure).
Details
Redox score ?
nan
PDB code
6sjv
Structure name
structure of hpv18 e6 oncoprotein in complex with mutant e6ap lxxll motif
Structure deposition date
2019-08-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
8
% buried
44
Peptide accession
Q05086
Residue number A
439
Residue number B
1138
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 439 of Ubiquitin-protein ligase E3A
Cysteine 1138 of Ubiquitin-protein ligase E3A
Cysteine 1138 in protein B could not be asigned to a Uniprot residue.
6sjv A 1035 A 1065
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 57 and 198 (1035 and 1065 respectively in this structure).
Details
Redox score ?
nan
PDB code
6sjv
Structure name
structure of hpv18 e6 oncoprotein in complex with mutant e6ap lxxll motif
Structure deposition date
2019-08-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
6
% buried
12
Peptide accession
Q05086
Residue number A
57
Residue number B
198
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 57 of Ubiquitin-protein ligase E3A
Cysteine 198 of Ubiquitin-protein ligase E3A
Uncertain whether structure cysteine 1065 has been assigned to correct residue.
6slm A 1106 A 1136
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 439 and 627 (1106 and 1136 respectively in this structure).
Details
Redox score ?
nan
PDB code
6slm
Structure name
crystal structure of full-length hpv31 e6 oncoprotein in complex with lxxll peptide of ubiquitin ligase e6ap
Structure deposition date
2019-08-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
56
Peptide accession
Q05086
Residue number A
439
Residue number B
627
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 439 of Ubiquitin-protein ligase E3A
Cysteine 627 of Ubiquitin-protein ligase E3A
Uncertain whether structure cysteine 1136 has been assigned to correct residue.
6slm A 1106 A 1139
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 439 and 1139 (1106 and 1139 respectively in this structure).
Details
Redox score ?
nan
PDB code
6slm
Structure name
crystal structure of full-length hpv31 e6 oncoprotein in complex with lxxll peptide of ubiquitin ligase e6ap
Structure deposition date
2019-08-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
62
Peptide accession
Q05086
Residue number A
439
Residue number B
1139
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 439 of Ubiquitin-protein ligase E3A
Cysteine 1139 of Ubiquitin-protein ligase E3A
Cysteine 1139 in protein B could not be asigned to a Uniprot residue.
6sjv A 1141 A 1142
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 843 and 1142 (1141 and 1142 respectively in this structure).
Details
Redox score ?
nan
PDB code
6sjv
Structure name
structure of hpv18 e6 oncoprotein in complex with mutant e6ap lxxll motif
Structure deposition date
2019-08-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
34
Minimum pKa ?
10
% buried
21
Peptide accession
Q05086
Residue number A
843
Residue number B
1142
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 843 of Ubiquitin-protein ligase E3A
Cysteine 1142 of Ubiquitin-protein ligase E3A
Cysteine 1142 in protein B could not be asigned to a Uniprot residue.
6sjv A 1105 A 1108
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 310 and 439 (1105 and 1108 respectively in this structure).
Details
Redox score ?
nan
PDB code
6sjv
Structure name
structure of hpv18 e6 oncoprotein in complex with mutant e6ap lxxll motif
Structure deposition date
2019-08-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
3
% buried
58
Peptide accession
Q05086
Residue number A
310
Residue number B
439
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 310 of Ubiquitin-protein ligase E3A
Cysteine 439 of Ubiquitin-protein ligase E3A
Uncertain whether structure cysteine 1105 has been assigned to correct residue.
6slm A 1033 A 1066
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 480 and 374 (1033 and 1066 respectively in this structure).
Details
Redox score ?
nan
PDB code
6slm
Structure name
crystal structure of full-length hpv31 e6 oncoprotein in complex with lxxll peptide of ubiquitin ligase e6ap
Structure deposition date
2019-08-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
22
Peptide accession
Q05086
Residue number A
480
Residue number B
374
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 480 of Ubiquitin-protein ligase E3A
Cysteine 374 of Ubiquitin-protein ligase E3A
Uncertain whether structure cysteine 1033 has been assigned to correct residue.
6sjv A 1105 A 1141
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 310 and 843 (1105 and 1141 respectively in this structure).
Details
Redox score ?
nan
PDB code
6sjv
Structure name
structure of hpv18 e6 oncoprotein in complex with mutant e6ap lxxll motif
Structure deposition date
2019-08-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
3
% buried
46
Peptide accession
Q05086
Residue number A
310
Residue number B
843
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 310 of Ubiquitin-protein ligase E3A
Cysteine 843 of Ubiquitin-protein ligase E3A
Uncertain whether structure cysteine 1105 has been assigned to correct residue.
6sjv A 1065 A 1068
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 198 and 374 (1065 and 1068 respectively in this structure).
Details
Redox score ?
nan
PDB code
6sjv
Structure name
structure of hpv18 e6 oncoprotein in complex with mutant e6ap lxxll motif
Structure deposition date
2019-08-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
14
Peptide accession
Q05086
Residue number A
198
Residue number B
374
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 198 of Ubiquitin-protein ligase E3A
Cysteine 374 of Ubiquitin-protein ligase E3A
Uncertain whether structure cysteine 1065 has been assigned to correct residue.
6sjv A 1105 A 1138
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 310 and 1138 (1105 and 1138 respectively in this structure).
Details
Redox score ?
nan
PDB code
6sjv
Structure name
structure of hpv18 e6 oncoprotein in complex with mutant e6ap lxxll motif
Structure deposition date
2019-08-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
3
% buried
47
Peptide accession
Q05086
Residue number A
310
Residue number B
1138
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 310 of Ubiquitin-protein ligase E3A
Cysteine 1138 of Ubiquitin-protein ligase E3A
Uncertain whether structure cysteine 1105 has been assigned to correct residue.
Cysteine 1138 in protein B could not be asigned to a Uniprot residue.
6slm A 1033 A 1063
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 480 and 1063 (1033 and 1063 respectively in this structure).
Details
Redox score ?
nan
PDB code
6slm
Structure name
crystal structure of full-length hpv31 e6 oncoprotein in complex with lxxll peptide of ubiquitin ligase e6ap
Structure deposition date
2019-08-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
8
% buried
22
Peptide accession
Q05086
Residue number A
480
Residue number B
1063
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 480 of Ubiquitin-protein ligase E3A
Cysteine 1063 of Ubiquitin-protein ligase E3A
Uncertain whether structure cysteine 1033 has been assigned to correct residue.
Cysteine 1063 in protein B could not be asigned to a Uniprot residue.
6sjv A 1105 A 1142
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 310 and 1142 (1105 and 1142 respectively in this structure).
Details
Redox score ?
nan
PDB code
6sjv
Structure name
structure of hpv18 e6 oncoprotein in complex with mutant e6ap lxxll motif
Structure deposition date
2019-08-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
53
Minimum pKa ?
3
% buried
36
Peptide accession
Q05086
Residue number A
310
Residue number B
1142
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 310 of Ubiquitin-protein ligase E3A
Cysteine 1142 of Ubiquitin-protein ligase E3A
Uncertain whether structure cysteine 1105 has been assigned to correct residue.
Cysteine 1142 in protein B could not be asigned to a Uniprot residue.
6slm A 1030 A 1066
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 1030 and 374 (1030 and 1066 respectively in this structure).
Details
Redox score ?
nan
PDB code
6slm
Structure name
crystal structure of full-length hpv31 e6 oncoprotein in complex with lxxll peptide of ubiquitin ligase e6ap
Structure deposition date
2019-08-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
6
% buried
45
Peptide accession
Q05086
Residue number A
1030
Residue number B
374
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 1030 of Ubiquitin-protein ligase E3A
Cysteine 374 of Ubiquitin-protein ligase E3A
Cysteine 1030 in protein A could not be asigned to a Uniprot residue.
6sjv A 1138 A 1141
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 1138 and 843 (1138 and 1141 respectively in this structure).
Details
Redox score ?
nan
PDB code
6sjv
Structure name
structure of hpv18 e6 oncoprotein in complex with mutant e6ap lxxll motif
Structure deposition date
2019-08-14
Thiol separation (Å)
3
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
32
Peptide accession
Q05086
Residue number A
1138
Residue number B
843
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 1138 of Ubiquitin-protein ligase E3A
Cysteine 843 of Ubiquitin-protein ligase E3A
Cysteine 1138 in protein A could not be asigned to a Uniprot residue.
6sjv A 1032 A 1068
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 1032 and 374 (1032 and 1068 respectively in this structure).
Details
Redox score ?
nan
PDB code
6sjv
Structure name
structure of hpv18 e6 oncoprotein in complex with mutant e6ap lxxll motif
Structure deposition date
2019-08-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
7
% buried
20
Peptide accession
Q05086
Residue number A
1032
Residue number B
374
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 1032 of Ubiquitin-protein ligase E3A
Cysteine 374 of Ubiquitin-protein ligase E3A
Cysteine 1032 in protein A could not be asigned to a Uniprot residue.
6slm A 1030 A 1033
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 1030 and 480 (1030 and 1033 respectively in this structure).
Details
Redox score ?
nan
PDB code
6slm
Structure name
crystal structure of full-length hpv31 e6 oncoprotein in complex with lxxll peptide of ubiquitin ligase e6ap
Structure deposition date
2019-08-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
6
% buried
34
Peptide accession
Q05086
Residue number A
1030
Residue number B
480
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 1030 of Ubiquitin-protein ligase E3A
Cysteine 480 of Ubiquitin-protein ligase E3A
Cysteine 1030 in protein A could not be asigned to a Uniprot residue.
Uncertain whether structure cysteine 1033 has been assigned to correct residue.
6sjv A 1032 A 1065
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 1032 and 198 (1032 and 1065 respectively in this structure).
Details
Redox score ?
nan
PDB code
6sjv
Structure name
structure of hpv18 e6 oncoprotein in complex with mutant e6ap lxxll motif
Structure deposition date
2019-08-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
7
% buried
24
Peptide accession
Q05086
Residue number A
1032
Residue number B
198
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 1032 of Ubiquitin-protein ligase E3A
Cysteine 198 of Ubiquitin-protein ligase E3A
Cysteine 1032 in protein A could not be asigned to a Uniprot residue.
Uncertain whether structure cysteine 1065 has been assigned to correct residue.
6slm A 1030 A 1063
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 1030 and 1063.
Details
Redox score ?
nan
PDB code
6slm
Structure name
crystal structure of full-length hpv31 e6 oncoprotein in complex with lxxll peptide of ubiquitin ligase e6ap
Structure deposition date
2019-08-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
6
% buried
44
Peptide accession
Q05086
Residue number A
1030
Residue number B
1063
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 1030 of Ubiquitin-protein ligase E3A
Cysteine 1063 of Ubiquitin-protein ligase E3A
Cysteine 1030 in protein A could not be asigned to a Uniprot residue.
Cysteine 1063 in protein B could not be asigned to a Uniprot residue.
6slm A 1063 A 1066
A redox-regulated disulphide may form within Ubiquitin-protein ligase E3A between cysteines 1063 and 374 (1063 and 1066 respectively in this structure).
Details
Redox score ?
nan
PDB code
6slm
Structure name
crystal structure of full-length hpv31 e6 oncoprotein in complex with lxxll peptide of ubiquitin ligase e6ap
Structure deposition date
2019-08-20
Thiol separation (Å)
3
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
34
Peptide accession
Q05086
Residue number A
1063
Residue number B
374
Peptide name
Ubiquitin-protein ligase E3A
Ligandability
Cysteine 1063 of Ubiquitin-protein ligase E3A
Cysteine 374 of Ubiquitin-protein ligase E3A
Cysteine 1063 in protein A could not be asigned to a Uniprot residue.
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