Cell growth-regulating nucleolar protein
Intramolecular
Cysteine 6 and cysteine 25
Cysteine 6 and cysteine 28
Cysteine 6 and cysteine 9
Cysteine 33 and cysteine 51
Cysteine 33 and cysteine 36
Cysteine 36 and cysteine 51
Cysteine 9 and cysteine 25
Cysteine 25 and cysteine 28
Cysteine 28 and cysteine 30
Cysteine 9 and cysteine 28
More...Cysteine 6 and cysteine 30
Cysteine 25 and cysteine 30
Cysteine 9 and cysteine 30
1wjv A 13 A 32
A redox-regulated disulphide may form within Cell growth-regulating nucleolar protein between cysteines 6 and 25 (13 and 32 respectively in this structure).
Details
Redox score ?
89
PDB code
1wjv
Structure name
solution structure of the n-terminal zinc finger domain of mouse cell growth regulating nucleolar protein lyar
Structure deposition date
2004-05-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
5
% buried
3
Peptide accession
Q08288
Residue number A
6
Residue number B
25
Peptide name
Cell growth-regulating nucleolar protein
Ligandability
Cysteine 6 of Cell growth-regulating nucleolar protein
Cysteine 25 of Cell growth-regulating nucleolar protein
1wjv A 13 A 35
A redox-regulated disulphide may form within Cell growth-regulating nucleolar protein between cysteines 6 and 28 (13 and 35 respectively in this structure).
Details
Redox score ?
85
PDB code
1wjv
Structure name
solution structure of the n-terminal zinc finger domain of mouse cell growth regulating nucleolar protein lyar
Structure deposition date
2004-05-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
5
% buried
11
Peptide accession
Q08288
Residue number A
6
Residue number B
28
Peptide name
Cell growth-regulating nucleolar protein
Ligandability
Cysteine 6 of Cell growth-regulating nucleolar protein
Cysteine 28 of Cell growth-regulating nucleolar protein
1wjv A 13 A 16
A redox-regulated disulphide may form within Cell growth-regulating nucleolar protein between cysteines 6 and 9 (13 and 16 respectively in this structure).
Details
Redox score ?
85
PDB code
1wjv
Structure name
solution structure of the n-terminal zinc finger domain of mouse cell growth regulating nucleolar protein lyar
Structure deposition date
2004-05-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
5
% buried
3
Peptide accession
Q08288
Residue number A
6
Residue number B
9
Peptide name
Cell growth-regulating nucleolar protein
Ligandability
Cysteine 6 of Cell growth-regulating nucleolar protein
Cysteine 9 of Cell growth-regulating nucleolar protein
1wjv A 40 A 58
A redox-regulated disulphide may form within Cell growth-regulating nucleolar protein between cysteines 33 and 51 (40 and 58 respectively in this structure).
Details
Redox score ?
85
PDB code
1wjv
Structure name
solution structure of the n-terminal zinc finger domain of mouse cell growth regulating nucleolar protein lyar
Structure deposition date
2004-05-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
7
% buried
7
Peptide accession
Q08288
Residue number A
33
Residue number B
51
Peptide name
Cell growth-regulating nucleolar protein
Ligandability
Cysteine 33 of Cell growth-regulating nucleolar protein
Cysteine 51 of Cell growth-regulating nucleolar protein
1wjv A 40 A 43
A redox-regulated disulphide may form within Cell growth-regulating nucleolar protein between cysteines 33 and 36 (40 and 43 respectively in this structure).
Details
Redox score ?
83
PDB code
1wjv
Structure name
solution structure of the n-terminal zinc finger domain of mouse cell growth regulating nucleolar protein lyar
Structure deposition date
2004-05-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
7
% buried
8
Peptide accession
Q08288
Residue number A
33
Residue number B
36
Peptide name
Cell growth-regulating nucleolar protein
Ligandability
Cysteine 33 of Cell growth-regulating nucleolar protein
Cysteine 36 of Cell growth-regulating nucleolar protein
1wjv A 43 A 58
A redox-regulated disulphide may form within Cell growth-regulating nucleolar protein between cysteines 36 and 51 (43 and 58 respectively in this structure).
Details
Redox score ?
80
PDB code
1wjv
Structure name
solution structure of the n-terminal zinc finger domain of mouse cell growth regulating nucleolar protein lyar
Structure deposition date
2004-05-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
9
% buried
1
Peptide accession
Q08288
Residue number A
36
Residue number B
51
Peptide name
Cell growth-regulating nucleolar protein
Ligandability
Cysteine 36 of Cell growth-regulating nucleolar protein
Cysteine 51 of Cell growth-regulating nucleolar protein
1wjv A 16 A 32
A redox-regulated disulphide may form within Cell growth-regulating nucleolar protein between cysteines 9 and 25 (16 and 32 respectively in this structure).
Details
Redox score ?
80
PDB code
1wjv
Structure name
solution structure of the n-terminal zinc finger domain of mouse cell growth regulating nucleolar protein lyar
Structure deposition date
2004-05-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
9
% buried
0
Peptide accession
Q08288
Residue number A
9
Residue number B
25
Peptide name
Cell growth-regulating nucleolar protein
Ligandability
Cysteine 9 of Cell growth-regulating nucleolar protein
Cysteine 25 of Cell growth-regulating nucleolar protein
1wjv A 32 A 35
A redox-regulated disulphide may form within Cell growth-regulating nucleolar protein between cysteines 25 and 28 (32 and 35 respectively in this structure).
Details
Redox score ?
69
PDB code
1wjv
Structure name
solution structure of the n-terminal zinc finger domain of mouse cell growth regulating nucleolar protein lyar
Structure deposition date
2004-05-29
Thiol separation (Å)
6
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
8
Peptide accession
Q08288
Residue number A
25
Residue number B
28
Peptide name
Cell growth-regulating nucleolar protein
Ligandability
Cysteine 25 of Cell growth-regulating nucleolar protein
Cysteine 28 of Cell growth-regulating nucleolar protein
1wjv A 35 A 37
A redox-regulated disulphide may form within Cell growth-regulating nucleolar protein between cysteines 28 and 30 (35 and 37 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
1wjv
Structure name
solution structure of the n-terminal zinc finger domain of mouse cell growth regulating nucleolar protein lyar
Structure deposition date
2004-05-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
9
Peptide accession
Q08288
Residue number A
28
Residue number B
30
Peptide name
Cell growth-regulating nucleolar protein
Ligandability
Cysteine 28 of Cell growth-regulating nucleolar protein
Cysteine 30 of Cell growth-regulating nucleolar protein
1wjv A 16 A 35
A redox-regulated disulphide may form within Cell growth-regulating nucleolar protein between cysteines 9 and 28 (16 and 35 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
1wjv
Structure name
solution structure of the n-terminal zinc finger domain of mouse cell growth regulating nucleolar protein lyar
Structure deposition date
2004-05-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
46
Minimum pKa ?
10
% buried
8
Peptide accession
Q08288
Residue number A
9
Residue number B
28
Peptide name
Cell growth-regulating nucleolar protein
Ligandability
Cysteine 9 of Cell growth-regulating nucleolar protein
Cysteine 28 of Cell growth-regulating nucleolar protein
1wjv A 13 A 37
A redox-regulated disulphide may form within Cell growth-regulating nucleolar protein between cysteines 6 and 30 (13 and 37 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
1wjv
Structure name
solution structure of the n-terminal zinc finger domain of mouse cell growth regulating nucleolar protein lyar
Structure deposition date
2004-05-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
5
% buried
4
Peptide accession
Q08288
Residue number A
6
Residue number B
30
Peptide name
Cell growth-regulating nucleolar protein
Ligandability
Cysteine 6 of Cell growth-regulating nucleolar protein
Cysteine 30 of Cell growth-regulating nucleolar protein
1wjv A 32 A 37
A redox-regulated disulphide may form within Cell growth-regulating nucleolar protein between cysteines 25 and 30 (32 and 37 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
1wjv
Structure name
solution structure of the n-terminal zinc finger domain of mouse cell growth regulating nucleolar protein lyar
Structure deposition date
2004-05-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
1
Peptide accession
Q08288
Residue number A
25
Residue number B
30
Peptide name
Cell growth-regulating nucleolar protein
Ligandability
Cysteine 25 of Cell growth-regulating nucleolar protein
Cysteine 30 of Cell growth-regulating nucleolar protein
1wjv A 16 A 37
A redox-regulated disulphide may form within Cell growth-regulating nucleolar protein between cysteines 9 and 30 (16 and 37 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
1wjv
Structure name
solution structure of the n-terminal zinc finger domain of mouse cell growth regulating nucleolar protein lyar
Structure deposition date
2004-05-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
44
Minimum pKa ?
10
% buried
1
Peptide accession
Q08288
Residue number A
9
Residue number B
30
Peptide name
Cell growth-regulating nucleolar protein
Ligandability
Cysteine 9 of Cell growth-regulating nucleolar protein
Cysteine 30 of Cell growth-regulating nucleolar protein
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