E3 ubiquitin-protein ligase TRIM33
Intramolecular
Cysteine 902 and cysteine 905
Cysteine 902 and cysteine 931
Cysteine 905 and cysteine 928
Cysteine 905 and cysteine 931
Cysteine 902 and cysteine 928
Cysteine 890 and cysteine 893
Cysteine 893 and cysteine 913
Cysteine 928 and cysteine 931
Cysteine 890 and cysteine 975
Cysteine 901 and cysteine 902
More...Cysteine 890 and cysteine 913
Cysteine 905 and cysteine 975
Cysteine 928 and cysteine 975
Cysteine 901 and cysteine 905
Cysteine 893 and cysteine 975
Cysteine 913 and cysteine 975
8bdy A 902 A 905
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM33 between cysteines 902 and 905.
Details
Redox score ?
84
PDB code
8bdy
Structure name
crystal structure of trim33 alpha phd-bromo domain in complex with 9
Structure deposition date
2022-10-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
6
% buried
28
Peptide accession
Q9UPN9
Residue number A
902
Residue number B
905
Peptide name
E3 ubiquitin-protein ligase TRIM33
Ligandability
Cysteine 902 of E3 ubiquitin-protein ligase TRIM33
Cysteine 905 of E3 ubiquitin-protein ligase TRIM33
8bd8 A 902 A 931
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM33 between cysteines 902 and 931.
Details
Redox score ?
84
PDB code
8bd8
Structure name
crystal structure of trim33 alpha phd-bromo domain in complex with 8
Structure deposition date
2022-10-18
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
7
% buried
26
Peptide accession
Q9UPN9
Residue number A
902
Residue number B
931
Peptide name
E3 ubiquitin-protein ligase TRIM33
Ligandability
Cysteine 902 of E3 ubiquitin-protein ligase TRIM33
Cysteine 931 of E3 ubiquitin-protein ligase TRIM33
3u5o B 905 B 928
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM33 between cysteines 905 and 928.
Details
Redox score ?
80
PDB code
3u5o
Structure name
crystal structure of the complex of trim33 phd-bromo and h3(1-22) k9me3k14ack18ac histone peptide
Structure deposition date
2011-10-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
6
% buried
66
Peptide accession
Q9UPN9
Residue number A
905
Residue number B
928
Peptide name
E3 ubiquitin-protein ligase TRIM33
Ligandability
Cysteine 905 of E3 ubiquitin-protein ligase TRIM33
Cysteine 928 of E3 ubiquitin-protein ligase TRIM33
3u5o F 905 F 931
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM33 between cysteines 905 and 931.
Details
Redox score ?
79
PDB code
3u5o
Structure name
crystal structure of the complex of trim33 phd-bromo and h3(1-22) k9me3k14ack18ac histone peptide
Structure deposition date
2011-10-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
42
Peptide accession
Q9UPN9
Residue number A
905
Residue number B
931
Peptide name
E3 ubiquitin-protein ligase TRIM33
Ligandability
Cysteine 905 of E3 ubiquitin-protein ligase TRIM33
Cysteine 931 of E3 ubiquitin-protein ligase TRIM33
3u5p H 902 H 928
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM33 between cysteines 902 and 928.
Details
Redox score ?
76
PDB code
3u5p
Structure name
crystal structure of the complex of trim33 phd-bromo and h3(1-28) k9me3k14ack18ack23ac histone peptide
Structure deposition date
2011-10-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
77
Minimum pKa ?
8
% buried
68
Peptide accession
Q9UPN9
Residue number A
902
Residue number B
928
Peptide name
E3 ubiquitin-protein ligase TRIM33
Ligandability
Cysteine 902 of E3 ubiquitin-protein ligase TRIM33
Cysteine 928 of E3 ubiquitin-protein ligase TRIM33
3u5o A 890 A 893
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM33 between cysteines 890 and 893.
Details
Redox score ?
75
PDB code
3u5o
Structure name
crystal structure of the complex of trim33 phd-bromo and h3(1-22) k9me3k14ack18ac histone peptide
Structure deposition date
2011-10-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
nan
Peptide accession
Q9UPN9
Residue number A
890
Residue number B
893
Peptide name
E3 ubiquitin-protein ligase TRIM33
Ligandability
Cysteine 890 of E3 ubiquitin-protein ligase TRIM33
Cysteine 893 of E3 ubiquitin-protein ligase TRIM33
3u5o H 893 H 913
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM33 between cysteines 893 and 913.
Details
Redox score ?
70
PDB code
3u5o
Structure name
crystal structure of the complex of trim33 phd-bromo and h3(1-22) k9me3k14ack18ac histone peptide
Structure deposition date
2011-10-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
64
Peptide accession
Q9UPN9
Residue number A
893
Residue number B
913
Peptide name
E3 ubiquitin-protein ligase TRIM33
Ligandability
Cysteine 893 of E3 ubiquitin-protein ligase TRIM33
Cysteine 913 of E3 ubiquitin-protein ligase TRIM33
3u5o G 928 G 931
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM33 between cysteines 928 and 931.
Details
Redox score ?
67
PDB code
3u5o
Structure name
crystal structure of the complex of trim33 phd-bromo and h3(1-22) k9me3k14ack18ac histone peptide
Structure deposition date
2011-10-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
62
Peptide accession
Q9UPN9
Residue number A
928
Residue number B
931
Peptide name
E3 ubiquitin-protein ligase TRIM33
Ligandability
Cysteine 928 of E3 ubiquitin-protein ligase TRIM33
Cysteine 931 of E3 ubiquitin-protein ligase TRIM33
3u5m L 890 L 975
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM33 between cysteines 890 and 975.
Details
Redox score ?
66
PDB code
3u5m
Structure name
crystal structure of trim33 phd-bromo in the free state
Structure deposition date
2011-10-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
58
Minimum pKa ?
2
% buried
64
Peptide accession
Q9UPN9
Residue number A
890
Residue number B
975
Peptide name
E3 ubiquitin-protein ligase TRIM33
Ligandability
Cysteine 890 of E3 ubiquitin-protein ligase TRIM33
Cysteine 975 of E3 ubiquitin-protein ligase TRIM33
3u5p D 901 D 902
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM33 between cysteines 901 and 902.
Details
Redox score ?
62
PDB code
3u5p
Structure name
crystal structure of the complex of trim33 phd-bromo and h3(1-28) k9me3k14ack18ack23ac histone peptide
Structure deposition date
2011-10-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
0
% buried
44
Peptide accession
Q9UPN9
Residue number A
901
Residue number B
902
Peptide name
E3 ubiquitin-protein ligase TRIM33
Ligandability
Cysteine 901 of E3 ubiquitin-protein ligase TRIM33
Cysteine 902 of E3 ubiquitin-protein ligase TRIM33
3u5o F 890 F 913
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM33 between cysteines 890 and 913. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
3u5o
Structure name
crystal structure of the complex of trim33 phd-bromo and h3(1-22) k9me3k14ack18ac histone peptide
Structure deposition date
2011-10-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
70
Minimum pKa ?
18
% buried
nan
Peptide accession
Q9UPN9
Residue number A
890
Residue number B
913
Peptide name
E3 ubiquitin-protein ligase TRIM33
Ligandability
Cysteine 890 of E3 ubiquitin-protein ligase TRIM33
Cysteine 913 of E3 ubiquitin-protein ligase TRIM33
5mr8 A 905 A 975
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM33 between cysteines 905 and 975. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
5mr8
Structure name
crystal structure of trim33 phd-bromodomain isoform b in complex with h3k9ac histone peptide
Structure deposition date
2016-12-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
52
Minimum pKa ?
8
% buried
64
Peptide accession
Q9UPN9
Residue number A
905
Residue number B
975
Peptide name
E3 ubiquitin-protein ligase TRIM33
Ligandability
Cysteine 905 of E3 ubiquitin-protein ligase TRIM33
Cysteine 975 of E3 ubiquitin-protein ligase TRIM33
3u5m K 928 K 975
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM33 between cysteines 928 and 975. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
3u5m
Structure name
crystal structure of trim33 phd-bromo in the free state
Structure deposition date
2011-10-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
74
Peptide accession
Q9UPN9
Residue number A
928
Residue number B
975
Peptide name
E3 ubiquitin-protein ligase TRIM33
Ligandability
Cysteine 928 of E3 ubiquitin-protein ligase TRIM33
Cysteine 975 of E3 ubiquitin-protein ligase TRIM33
3u5m L 901 L 905
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM33 between cysteines 901 and 905. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
3u5m
Structure name
crystal structure of trim33 phd-bromo in the free state
Structure deposition date
2011-10-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
12
Peptide accession
Q9UPN9
Residue number A
901
Residue number B
905
Peptide name
E3 ubiquitin-protein ligase TRIM33
Ligandability
Cysteine 901 of E3 ubiquitin-protein ligase TRIM33
Cysteine 905 of E3 ubiquitin-protein ligase TRIM33
3u5o B 893 B 975
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM33 between cysteines 893 and 975. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
3u5o
Structure name
crystal structure of the complex of trim33 phd-bromo and h3(1-22) k9me3k14ack18ac histone peptide
Structure deposition date
2011-10-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
80
Peptide accession
Q9UPN9
Residue number A
893
Residue number B
975
Peptide name
E3 ubiquitin-protein ligase TRIM33
Ligandability
Cysteine 893 of E3 ubiquitin-protein ligase TRIM33
Cysteine 975 of E3 ubiquitin-protein ligase TRIM33
3u5m J 913 J 975
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM33 between cysteines 913 and 975. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
3u5m
Structure name
crystal structure of trim33 phd-bromo in the free state
Structure deposition date
2011-10-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
12
% buried
68
Peptide accession
Q9UPN9
Residue number A
913
Residue number B
975
Peptide name
E3 ubiquitin-protein ligase TRIM33
Ligandability
Cysteine 913 of E3 ubiquitin-protein ligase TRIM33
Cysteine 975 of E3 ubiquitin-protein ligase TRIM33
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