E3 ubiquitin-protein ligase Midline-1
Intramolecular
Cysteine 119 and cysteine 122
Cysteine 134 and cysteine 137
Cysteine 119 and cysteine 142
Cysteine 175 and cysteine 198
Cysteine 122 and cysteine 142
Cysteine 119 and cysteine 145
Cysteine 122 and cysteine 145
Cysteine 142 and cysteine 145
Cysteine 195 and cysteine 198
Cysteine 175 and cysteine 195
More...Cysteine 578 and cysteine 580
Cysteine 175 and cysteine 187
Cysteine 187 and cysteine 195
Cysteine 187 and cysteine 198
2jun A 119 A 122
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Midline-1 between cysteines 119 and 122.
Details
Redox score ?
87
PDB code
2jun
Structure name
structure of the mid1 tandem b-boxes reveals an interaction reminiscent of intermolecular ring heterodimers
Structure deposition date
2007-08-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
4
Peptide accession
O15344
Residue number A
119
Residue number B
122
Peptide name
E3 ubiquitin-protein ligase Midline-1
Ligandability
Cysteine 119 of E3 ubiquitin-protein ligase Midline-1
Cysteine 122 of E3 ubiquitin-protein ligase Midline-1
2ffw A 134 A 137
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Midline-1 between cysteines 134 and 137.
Details
Redox score ?
86
PDB code
2ffw
Structure name
solution structure of the rbcc/trim b-box1 domain of human mid1: b-box with a ring
Structure deposition date
2005-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
6
% buried
0
Peptide accession
O15344
Residue number A
134
Residue number B
137
Peptide name
E3 ubiquitin-protein ligase Midline-1
Ligandability
Cysteine 134 of E3 ubiquitin-protein ligase Midline-1
Cysteine 137 of E3 ubiquitin-protein ligase Midline-1
2ffw A 119 A 142
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Midline-1 between cysteines 119 and 142.
Details
Redox score ?
85
PDB code
2ffw
Structure name
solution structure of the rbcc/trim b-box1 domain of human mid1: b-box with a ring
Structure deposition date
2005-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
2
Peptide accession
O15344
Residue number A
119
Residue number B
142
Peptide name
E3 ubiquitin-protein ligase Midline-1
Ligandability
Cysteine 119 of E3 ubiquitin-protein ligase Midline-1
Cysteine 142 of E3 ubiquitin-protein ligase Midline-1
2dq5 A 175 A 198
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Midline-1 between cysteines 175 and 198.
Details
Redox score ?
84
PDB code
2dq5
Structure name
solution structure of the mid1 b box2 chc(d/c)c2h2 zinc-binding domain: insights into an evolutionary conserved ring fold
Structure deposition date
2006-05-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
0
Peptide accession
O15344
Residue number A
175
Residue number B
198
Peptide name
E3 ubiquitin-protein ligase Midline-1
Ligandability
Cysteine 175 of E3 ubiquitin-protein ligase Midline-1
Cysteine 198 of E3 ubiquitin-protein ligase Midline-1
2ffw A 122 A 142
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Midline-1 between cysteines 122 and 142.
Details
Redox score ?
82
PDB code
2ffw
Structure name
solution structure of the rbcc/trim b-box1 domain of human mid1: b-box with a ring
Structure deposition date
2005-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
0
Peptide accession
O15344
Residue number A
122
Residue number B
142
Peptide name
E3 ubiquitin-protein ligase Midline-1
Ligandability
Cysteine 122 of E3 ubiquitin-protein ligase Midline-1
Cysteine 142 of E3 ubiquitin-protein ligase Midline-1
2jun A 119 A 145
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Midline-1 between cysteines 119 and 145.
Details
Redox score ?
82
PDB code
2jun
Structure name
structure of the mid1 tandem b-boxes reveals an interaction reminiscent of intermolecular ring heterodimers
Structure deposition date
2007-08-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
4
Peptide accession
O15344
Residue number A
119
Residue number B
145
Peptide name
E3 ubiquitin-protein ligase Midline-1
Ligandability
Cysteine 119 of E3 ubiquitin-protein ligase Midline-1
Cysteine 145 of E3 ubiquitin-protein ligase Midline-1
2ffw A 122 A 145
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Midline-1 between cysteines 122 and 145.
Details
Redox score ?
80
PDB code
2ffw
Structure name
solution structure of the rbcc/trim b-box1 domain of human mid1: b-box with a ring
Structure deposition date
2005-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
0
Peptide accession
O15344
Residue number A
122
Residue number B
145
Peptide name
E3 ubiquitin-protein ligase Midline-1
Ligandability
Cysteine 122 of E3 ubiquitin-protein ligase Midline-1
Cysteine 145 of E3 ubiquitin-protein ligase Midline-1
2ffw A 142 A 145
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Midline-1 between cysteines 142 and 145.
Details
Redox score ?
79
PDB code
2ffw
Structure name
solution structure of the rbcc/trim b-box1 domain of human mid1: b-box with a ring
Structure deposition date
2005-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
0
Peptide accession
O15344
Residue number A
142
Residue number B
145
Peptide name
E3 ubiquitin-protein ligase Midline-1
Ligandability
Cysteine 142 of E3 ubiquitin-protein ligase Midline-1
Cysteine 145 of E3 ubiquitin-protein ligase Midline-1
2dq5 A 195 A 198
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Midline-1 between cysteines 195 and 198.
Details
Redox score ?
78
PDB code
2dq5
Structure name
solution structure of the mid1 b box2 chc(d/c)c2h2 zinc-binding domain: insights into an evolutionary conserved ring fold
Structure deposition date
2006-05-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
0
Peptide accession
O15344
Residue number A
195
Residue number B
198
Peptide name
E3 ubiquitin-protein ligase Midline-1
Ligandability
Cysteine 195 of E3 ubiquitin-protein ligase Midline-1
Cysteine 198 of E3 ubiquitin-protein ligase Midline-1
2jun A 175 A 195
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Midline-1 between cysteines 175 and 195.
Details
Redox score ?
75
PDB code
2jun
Structure name
structure of the mid1 tandem b-boxes reveals an interaction reminiscent of intermolecular ring heterodimers
Structure deposition date
2007-08-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
26
Peptide accession
O15344
Residue number A
175
Residue number B
195
Peptide name
E3 ubiquitin-protein ligase Midline-1
Ligandability
Cysteine 175 of E3 ubiquitin-protein ligase Midline-1
Cysteine 195 of E3 ubiquitin-protein ligase Midline-1
7qry C 578 C 580
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Midline-1 between cysteines 578 and 580. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
7qry
Structure name
crystal structure of b30
Structure deposition date
2022-01-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
64
Peptide accession
O15344
Residue number A
578
Residue number B
580
Peptide name
E3 ubiquitin-protein ligase Midline-1
Ligandability
Cysteine 578 of E3 ubiquitin-protein ligase Midline-1
Cysteine 580 of E3 ubiquitin-protein ligase Midline-1
2dq5 A 175 A 187
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Midline-1 between cysteines 175 and 187. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
2dq5
Structure name
solution structure of the mid1 b box2 chc(d/c)c2h2 zinc-binding domain: insights into an evolutionary conserved ring fold
Structure deposition date
2006-05-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
46
Minimum pKa ?
7
% buried
0
Peptide accession
O15344
Residue number A
175
Residue number B
187
Peptide name
E3 ubiquitin-protein ligase Midline-1
Ligandability
Cysteine 175 of E3 ubiquitin-protein ligase Midline-1
Cysteine 187 of E3 ubiquitin-protein ligase Midline-1
2dq5 A 187 A 195
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Midline-1 between cysteines 187 and 195. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
2dq5
Structure name
solution structure of the mid1 b box2 chc(d/c)c2h2 zinc-binding domain: insights into an evolutionary conserved ring fold
Structure deposition date
2006-05-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
0
Peptide accession
O15344
Residue number A
187
Residue number B
195
Peptide name
E3 ubiquitin-protein ligase Midline-1
Ligandability
Cysteine 187 of E3 ubiquitin-protein ligase Midline-1
Cysteine 195 of E3 ubiquitin-protein ligase Midline-1
2jun A 187 A 198
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Midline-1 between cysteines 187 and 198. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
2jun
Structure name
structure of the mid1 tandem b-boxes reveals an interaction reminiscent of intermolecular ring heterodimers
Structure deposition date
2007-08-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
37
Peptide accession
O15344
Residue number A
187
Residue number B
198
Peptide name
E3 ubiquitin-protein ligase Midline-1
Ligandability
Cysteine 187 of E3 ubiquitin-protein ligase Midline-1
Cysteine 198 of E3 ubiquitin-protein ligase Midline-1
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