E3 ubiquitin-protein ligase TRIM23
Intramolecular
Cysteine 51 and cysteine 72
Cysteine 31 and cysteine 34
Cysteine 34 and cysteine 59
Cysteine 34 and cysteine 56
Cysteine 31 and cysteine 56
Cysteine 56 and cysteine 59
Cysteine 31 and cysteine 59
5vzv A 51 A 72
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM23 between cysteines 51 and 72.
Details
Redox score ?
84
PDB code
5vzv
Structure name
trim23 ring domain
Structure deposition date
2017-05-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
4
% buried
68
Peptide accession
P36406
Residue number A
51
Residue number B
72
Peptide name
E3 ubiquitin-protein ligase TRIM23
Ligandability
Cysteine 51 of E3 ubiquitin-protein ligase TRIM23
Cysteine 72 of E3 ubiquitin-protein ligase TRIM23
5vzv A 31 A 34
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM23 between cysteines 31 and 34.
Details
Redox score ?
81
PDB code
5vzv
Structure name
trim23 ring domain
Structure deposition date
2017-05-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
40
Peptide accession
P36406
Residue number A
31
Residue number B
34
Peptide name
E3 ubiquitin-protein ligase TRIM23
Ligandability
Cysteine 31 of E3 ubiquitin-protein ligase TRIM23
Cysteine 34 of E3 ubiquitin-protein ligase TRIM23
5vzw G 34 G 59
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM23 between cysteines 34 and 59.
Details
Redox score ?
80
PDB code
5vzw
Structure name
trim23 ring domain in complex with ubch5-ub
Structure deposition date
2017-05-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
5
% buried
68
Peptide accession
P36406
Residue number A
34
Residue number B
59
Peptide name
E3 ubiquitin-protein ligase TRIM23
Ligandability
Cysteine 34 of E3 ubiquitin-protein ligase TRIM23
Cysteine 59 of E3 ubiquitin-protein ligase TRIM23
5vzw G 34 G 56
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM23 between cysteines 34 and 56.
Details
Redox score ?
76
PDB code
5vzw
Structure name
trim23 ring domain in complex with ubch5-ub
Structure deposition date
2017-05-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
5
% buried
62
Peptide accession
P36406
Residue number A
34
Residue number B
56
Peptide name
E3 ubiquitin-protein ligase TRIM23
Ligandability
Cysteine 34 of E3 ubiquitin-protein ligase TRIM23
Cysteine 56 of E3 ubiquitin-protein ligase TRIM23
5vzv A 31 A 56
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM23 between cysteines 31 and 56.
Details
Redox score ?
74
PDB code
5vzv
Structure name
trim23 ring domain
Structure deposition date
2017-05-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
8
% buried
50
Peptide accession
P36406
Residue number A
31
Residue number B
56
Peptide name
E3 ubiquitin-protein ligase TRIM23
Ligandability
Cysteine 31 of E3 ubiquitin-protein ligase TRIM23
Cysteine 56 of E3 ubiquitin-protein ligase TRIM23
5vzv C 56 C 59
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM23 between cysteines 56 and 59.
Details
Redox score ?
74
PDB code
5vzv
Structure name
trim23 ring domain
Structure deposition date
2017-05-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
26
Peptide accession
P36406
Residue number A
56
Residue number B
59
Peptide name
E3 ubiquitin-protein ligase TRIM23
Ligandability
Cysteine 56 of E3 ubiquitin-protein ligase TRIM23
Cysteine 59 of E3 ubiquitin-protein ligase TRIM23
5vzw G 31 G 59
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM23 between cysteines 31 and 59. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
5vzw
Structure name
trim23 ring domain in complex with ubch5-ub
Structure deposition date
2017-05-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
23
% buried
nan
Peptide accession
P36406
Residue number A
31
Residue number B
59
Peptide name
E3 ubiquitin-protein ligase TRIM23
Ligandability
Cysteine 31 of E3 ubiquitin-protein ligase TRIM23
Cysteine 59 of E3 ubiquitin-protein ligase TRIM23
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