E3 ubiquitin-protein ligase RING2
Intramolecular
Cysteine 87 and cysteine 90
Cysteine 67 and cysteine 87
Cysteine 51 and cysteine 72
Cysteine 51 and cysteine 54
Cysteine 54 and cysteine 75
Cysteine 54 and cysteine 72
Cysteine 67 and cysteine 90
Cysteine 72 and cysteine 75
Cysteine 51 and cysteine 75
2h0d B 87 B 90
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RING2 between cysteines 87 and 90.
Details
Redox score ?
89
PDB code
2h0d
Structure name
structure of a bmi-1-ring1b polycomb group ubiquitin ligase complex
Structure deposition date
2006-05-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
3
% buried
24
Peptide accession
Q99496
Residue number A
87
Residue number B
90
Peptide name
E3 ubiquitin-protein ligase RING2
Ligandability
Cysteine 87 of E3 ubiquitin-protein ligase RING2
Cysteine 90 of E3 ubiquitin-protein ligase RING2
2h0d B 67 B 87
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RING2 between cysteines 67 and 87.
Details
Redox score ?
86
PDB code
2h0d
Structure name
structure of a bmi-1-ring1b polycomb group ubiquitin ligase complex
Structure deposition date
2006-05-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
3
% buried
45
Peptide accession
Q99496
Residue number A
67
Residue number B
87
Peptide name
E3 ubiquitin-protein ligase RING2
Ligandability
Cysteine 67 of E3 ubiquitin-protein ligase RING2
Cysteine 87 of E3 ubiquitin-protein ligase RING2
2h0d B 51 B 72
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RING2 between cysteines 51 and 72.
Details
Redox score ?
85
PDB code
2h0d
Structure name
structure of a bmi-1-ring1b polycomb group ubiquitin ligase complex
Structure deposition date
2006-05-14
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
6
% buried
25
Peptide accession
Q99496
Residue number A
51
Residue number B
72
Peptide name
E3 ubiquitin-protein ligase RING2
Ligandability
Cysteine 51 of E3 ubiquitin-protein ligase RING2
Cysteine 72 of E3 ubiquitin-protein ligase RING2
2ckl B 51 B 54
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RING2 between cysteines 51 and 54.
Details
Redox score ?
84
PDB code
2ckl
Structure name
ring1b-bmi1 e3 catalytic domain structure
Structure deposition date
2006-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
6
% buried
16
Peptide accession
Q9CQJ4
Residue number A
51
Residue number B
54
Peptide name
E3 ubiquitin-protein ligase RING2
Ligandability
Cysteine 51 of E3 ubiquitin-protein ligase RING2
Cysteine 54 of E3 ubiquitin-protein ligase RING2
4s3o B 54 B 75
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RING2 between cysteines 54 and 75.
Details
Redox score ?
78
PDB code
4s3o
Structure name
pcgf5-ring1b-ubch5c complex
Structure deposition date
2015-03-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
6
% buried
56
Peptide accession
Q99496
Residue number A
54
Residue number B
75
Peptide name
E3 ubiquitin-protein ligase RING2
Ligandability
Cysteine 54 of E3 ubiquitin-protein ligase RING2
Cysteine 75 of E3 ubiquitin-protein ligase RING2
2ckl B 54 B 72
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RING2 between cysteines 54 and 72.
Details
Redox score ?
78
PDB code
2ckl
Structure name
ring1b-bmi1 e3 catalytic domain structure
Structure deposition date
2006-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
11
Peptide accession
Q9CQJ4
Residue number A
54
Residue number B
72
Peptide name
E3 ubiquitin-protein ligase RING2
Ligandability
Cysteine 54 of E3 ubiquitin-protein ligase RING2
Cysteine 72 of E3 ubiquitin-protein ligase RING2
2h0d B 67 B 90
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RING2 between cysteines 67 and 90.
Details
Redox score ?
78
PDB code
2h0d
Structure name
structure of a bmi-1-ring1b polycomb group ubiquitin ligase complex
Structure deposition date
2006-05-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
26
Peptide accession
Q99496
Residue number A
67
Residue number B
90
Peptide name
E3 ubiquitin-protein ligase RING2
Ligandability
Cysteine 67 of E3 ubiquitin-protein ligase RING2
Cysteine 90 of E3 ubiquitin-protein ligase RING2
2ckl B 72 B 75
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RING2 between cysteines 72 and 75.
Details
Redox score ?
71
PDB code
2ckl
Structure name
ring1b-bmi1 e3 catalytic domain structure
Structure deposition date
2006-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
15
Peptide accession
Q9CQJ4
Residue number A
72
Residue number B
75
Peptide name
E3 ubiquitin-protein ligase RING2
Ligandability
Cysteine 72 of E3 ubiquitin-protein ligase RING2
Cysteine 75 of E3 ubiquitin-protein ligase RING2
4s3o E 51 E 75
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RING2 between cysteines 51 and 75. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
4s3o
Structure name
pcgf5-ring1b-ubch5c complex
Structure deposition date
2015-03-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
22
% buried
nan
Peptide accession
Q99496
Residue number A
51
Residue number B
75
Peptide name
E3 ubiquitin-protein ligase RING2
Ligandability
Cysteine 51 of E3 ubiquitin-protein ligase RING2
Cysteine 75 of E3 ubiquitin-protein ligase RING2
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