Ribonuclease H2 subunit A
Intramolecular
Cysteine 24 and cysteine 29
Cysteine 24 and cysteine 52
Cysteine 50 and cysteine 181
Cysteine 29 and cysteine 52
Cysteine 24 and cysteine 50
Cysteine 50 and cysteine 52
Cysteine 29 and cysteine 50
3puf M 24 M 29
A redox-regulated disulphide may form within Ribonuclease H2 subunit A between cysteines 24 and 29.
Details
Redox score ?
80
PDB code
3puf
Structure name
crystal structure of human rnase h2 complex
Structure deposition date
2010-12-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
8
% buried
52
Peptide accession
O75792
Residue number A
24
Residue number B
29
Peptide name
Ribonuclease H2 subunit A
Ligandability
Cysteine 24 of Ribonuclease H2 subunit A
Cysteine 29 of Ribonuclease H2 subunit A
3puf J 24 J 52
A redox-regulated disulphide may form within Ribonuclease H2 subunit A between cysteines 24 and 52.
Details
Redox score ?
60
PDB code
3puf
Structure name
crystal structure of human rnase h2 complex
Structure deposition date
2010-12-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
7
% buried
46
Peptide accession
O75792
Residue number A
24
Residue number B
52
Peptide name
Ribonuclease H2 subunit A
Ligandability
Cysteine 24 of Ribonuclease H2 subunit A
Cysteine 52 of Ribonuclease H2 subunit A
3puf J 50 J 181
A redox-regulated disulphide may form within Ribonuclease H2 subunit A between cysteines 50 and 181. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
3puf
Structure name
crystal structure of human rnase h2 complex
Structure deposition date
2010-12-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
96
Minimum pKa ?
9
% buried
96
Peptide accession
O75792
Residue number A
50
Residue number B
181
Peptide name
Ribonuclease H2 subunit A
Ligandability
Cysteine 50 of Ribonuclease H2 subunit A
Cysteine 181 of Ribonuclease H2 subunit A
3p56 A 29 A 52
A redox-regulated disulphide may form within Ribonuclease H2 subunit A between cysteines 29 and 52. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
3p56
Structure name
the structure of the human rnase h2 complex defines key interaction interfaces relevant to enzyme function and human disease
Structure deposition date
2010-10-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
48
Peptide accession
O75792
Residue number A
29
Residue number B
52
Peptide name
Ribonuclease H2 subunit A
Ligandability
Cysteine 29 of Ribonuclease H2 subunit A
Cysteine 52 of Ribonuclease H2 subunit A
3p56 A 24 A 50
A redox-regulated disulphide may form within Ribonuclease H2 subunit A between cysteines 24 and 50. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
3p56
Structure name
the structure of the human rnase h2 complex defines key interaction interfaces relevant to enzyme function and human disease
Structure deposition date
2010-10-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
10
% buried
70
Peptide accession
O75792
Residue number A
24
Residue number B
50
Peptide name
Ribonuclease H2 subunit A
Ligandability
Cysteine 24 of Ribonuclease H2 subunit A
Cysteine 50 of Ribonuclease H2 subunit A
3puf J 50 J 52
A redox-regulated disulphide may form within Ribonuclease H2 subunit A between cysteines 50 and 52. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
3puf
Structure name
crystal structure of human rnase h2 complex
Structure deposition date
2010-12-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
94
Minimum pKa ?
11
% buried
75
Peptide accession
O75792
Residue number A
50
Residue number B
52
Peptide name
Ribonuclease H2 subunit A
Ligandability
Cysteine 50 of Ribonuclease H2 subunit A
Cysteine 52 of Ribonuclease H2 subunit A
3puf A 29 A 50
A redox-regulated disulphide may form within Ribonuclease H2 subunit A between cysteines 29 and 50. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
23
PDB code
3puf
Structure name
crystal structure of human rnase h2 complex
Structure deposition date
2010-12-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
90
Minimum pKa ?
14
% buried
78
Peptide accession
O75792
Residue number A
29
Residue number B
50
Peptide name
Ribonuclease H2 subunit A
Ligandability
Cysteine 29 of Ribonuclease H2 subunit A
Cysteine 50 of Ribonuclease H2 subunit A
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