TP53-binding protein 1
Intermolecular
Cysteine 1525 and cysteine 1525
Intramolecular
Cysteine 1796 and cysteine 1802
Cysteine 1796 and cysteine 1818
Cysteine 1818 and cysteine 1825
Cysteine 1926 and cysteine 1933
Cysteine 1810 and cysteine 1825
Cysteine 1802 and cysteine 1818
Cysteine 1810 and cysteine 1818
4cri A 1525 B 1525
A redox-regulated disulphide may form between two units of TP53-binding protein 1 at cysteines 1525 and 1525.
Details
Redox score ?
77
PDB code
4cri
Structure name
crystal structure of 53bp1 tandem tudor domains in complex with methylated k810 rb peptide
Structure deposition date
2014-02-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide A name
TP53-binding protein 1
Peptide B name
TP53-binding protein 1
Peptide A accession
Q12888
Peptide B accession
Q12888
Peptide A residue number
1525
Peptide B residue number
1525
Ligandability
5ecg C 1796 C 1802
A redox-regulated disulphide may form within TP53-binding protein 1 between cysteines 1796 and 1802.
Details
Redox score ?
87
PDB code
5ecg
Structure name
crystal structure of the brct domains of 53bp1 in complex with p53 and h2ax-pser139 (gammah2ax)
Structure deposition date
2015-10-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q12888
Residue number A
1796
Residue number B
1802
Peptide name
TP53-binding protein 1
Ligandability
Cysteine 1796 of TP53-binding protein 1
Cysteine 1802 of TP53-binding protein 1
1kzy C 1796 C 1818
A redox-regulated disulphide may form within TP53-binding protein 1 between cysteines 1796 and 1818. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
1kzy
Structure name
crystal structure of the 53bp1 brct region complexed to tumor suppressor p53
Structure deposition date
2002-02-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
69
Peptide accession
Q12888
Residue number A
1796
Residue number B
1818
Peptide name
TP53-binding protein 1
Ligandability
Cysteine 1796 of TP53-binding protein 1
Cysteine 1818 of TP53-binding protein 1
1kzy C 1818 C 1825
A redox-regulated disulphide may form within TP53-binding protein 1 between cysteines 1818 and 1825. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
1kzy
Structure name
crystal structure of the 53bp1 brct region complexed to tumor suppressor p53
Structure deposition date
2002-02-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
100
Peptide accession
Q12888
Residue number A
1818
Residue number B
1825
Peptide name
TP53-binding protein 1
Ligandability
Cysteine 1818 of TP53-binding protein 1
Cysteine 1825 of TP53-binding protein 1
1gzh D 1926 D 1933
A redox-regulated disulphide may form within TP53-binding protein 1 between cysteines 1926 and 1933. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
1gzh
Structure name
crystal structure of the brct domains of human 53bp1 bound to the p53 tumor supressor
Structure deposition date
2002-05-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
25
Peptide accession
Q12888
Residue number A
1926
Residue number B
1933
Peptide name
TP53-binding protein 1
Ligandability
Cysteine 1926 of TP53-binding protein 1
Cysteine 1933 of TP53-binding protein 1
5ecg C 1810 C 1825
A redox-regulated disulphide may form within TP53-binding protein 1 between cysteines 1810 and 1825. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
5ecg
Structure name
crystal structure of the brct domains of 53bp1 in complex with p53 and h2ax-pser139 (gammah2ax)
Structure deposition date
2015-10-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
88
Peptide accession
Q12888
Residue number A
1810
Residue number B
1825
Peptide name
TP53-binding protein 1
Ligandability
Cysteine 1810 of TP53-binding protein 1
Cysteine 1825 of TP53-binding protein 1
5ecg C 1802 C 1818
A redox-regulated disulphide may form within TP53-binding protein 1 between cysteines 1802 and 1818. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
5ecg
Structure name
crystal structure of the brct domains of 53bp1 in complex with p53 and h2ax-pser139 (gammah2ax)
Structure deposition date
2015-10-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
14
% buried
nan
Peptide accession
Q12888
Residue number A
1802
Residue number B
1818
Peptide name
TP53-binding protein 1
Ligandability
Cysteine 1802 of TP53-binding protein 1
Cysteine 1818 of TP53-binding protein 1
1gzh D 1810 D 1818
A redox-regulated disulphide may form within TP53-binding protein 1 between cysteines 1810 and 1818. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
1gzh
Structure name
crystal structure of the brct domains of human 53bp1 bound to the p53 tumor supressor
Structure deposition date
2002-05-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
78
Peptide accession
Q12888
Residue number A
1810
Residue number B
1818
Peptide name
TP53-binding protein 1
Ligandability
Cysteine 1810 of TP53-binding protein 1
Cysteine 1818 of TP53-binding protein 1
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