Tumor protein p73
Intermolecular
Cysteine 194 and cysteine 194
Intramolecular
Cysteine 79 and cysteine 619
Cysteine 194 and cysteine 262
Cysteine 258 and cysteine 262
Cysteine 194 and cysteine 258
Cysteine 153 and cysteine 159
Cysteine 502 and cysteine 505
Cysteine 295 and cysteine 297
Cysteine 153 and cysteine 295
Cysteine 159 and cysteine 295
More...Cysteine 74 and cysteine 619
Cysteine 74 and cysteine 79
Cysteine 26 and cysteine 31
Cysteine 49 and cysteine 502
Cysteine 49 and cysteine 505
7ezj a 194 b 194
A redox-regulated disulphide may form between two units of Tumor protein p73 at cysteines 194 and 194. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
7ezj
Structure name
crystal structure of p73 dna binding domain complex bound with 1 bp and 2 bp spacer dna response elements
Structure deposition date
2021-06-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
7
% buried
nan
Peptide A name
Tumor protein p73
Peptide B name
Tumor protein p73
Peptide A accession
O15350
Peptide B accession
O15350
Peptide A residue number
194
Peptide B residue number
194
Ligandability
6fgs A 79 A 84
A redox-regulated disulphide may form within Tumor protein p73 between cysteines 79 and 619 (79 and 84 respectively in this structure).
Details
Redox score ?
88
PDB code
6fgs
Structure name
solution structure of p300taz2-p73ta1
Structure deposition date
2018-01-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
12
Peptide accession
O15350
Residue number A
79
Residue number B
619
Peptide name
Tumor protein p73
Ligandability
Cysteine 79 of Tumor protein p73
Cysteine 619 of Tumor protein p73
Cysteine 79 in protein A could not be asigned to a Uniprot residue.
3vd1 A 194 A 262
A redox-regulated disulphide may form within Tumor protein p73 between cysteines 194 and 262.
Details
Redox score ?
80
PDB code
3vd1
Structure name
structure of p73 dna binding domain tetramer modulates p73 transactivation
Structure deposition date
2012-01-04
Thiol separation (Å)
3
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
74
Peptide accession
O15350
Residue number A
194
Residue number B
262
Peptide name
Tumor protein p73
Ligandability
Cysteine 194 of Tumor protein p73
Cysteine 262 of Tumor protein p73
4guo I 258 I 262
A redox-regulated disulphide may form within Tumor protein p73 between cysteines 258 and 262.
Details
Redox score ?
76
PDB code
4guo
Structure name
structure of p73 dna binding domain complex with 12 bp dna
Structure deposition date
2012-08-29
Thiol separation (Å)
3
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
90
Peptide accession
O15350
Residue number A
258
Residue number B
262
Peptide name
Tumor protein p73
Ligandability
Cysteine 258 of Tumor protein p73
Cysteine 262 of Tumor protein p73
4guo I 194 I 258
A redox-regulated disulphide may form within Tumor protein p73 between cysteines 194 and 258.
Details
Redox score ?
75
PDB code
4guo
Structure name
structure of p73 dna binding domain complex with 12 bp dna
Structure deposition date
2012-08-29
Thiol separation (Å)
3
Half-sphere exposure sum ?
78
Minimum pKa ?
10
% buried
nan
Peptide accession
O15350
Residue number A
194
Residue number B
258
Peptide name
Tumor protein p73
Ligandability
Cysteine 194 of Tumor protein p73
Cysteine 258 of Tumor protein p73
3vd2 A 153 A 159
A redox-regulated disulphide may form within Tumor protein p73 between cysteines 153 and 159.
Details
Redox score ?
73
PDB code
3vd2
Structure name
structure of p73 dna binding domain tetramer modulates p73 transactivation
Structure deposition date
2012-01-04
Thiol separation (Å)
3
Half-sphere exposure sum ?
75
Minimum pKa ?
9
% buried
99
Peptide accession
O15350
Residue number A
153
Residue number B
159
Peptide name
Tumor protein p73
Ligandability
Cysteine 153 of Tumor protein p73
Cysteine 159 of Tumor protein p73
1dxs A 16 A 19
A redox-regulated disulphide may form within Tumor protein p73 between cysteines 502 and 505 (16 and 19 respectively in this structure).
Details
Redox score ?
72
PDB code
1dxs
Structure name
crystal structure of the c-terminal sterile alpha motif (sam) domain of human p73 alpha splice variant
Structure deposition date
2000-01-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
21
Peptide accession
O15350
Residue number A
502
Residue number B
505
Peptide name
Tumor protein p73
Ligandability
Cysteine 502 of Tumor protein p73
Cysteine 505 of Tumor protein p73
3vd2 D 295 D 297
A redox-regulated disulphide may form within Tumor protein p73 between cysteines 295 and 297. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
3vd2
Structure name
structure of p73 dna binding domain tetramer modulates p73 transactivation
Structure deposition date
2012-01-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
86
Peptide accession
O15350
Residue number A
295
Residue number B
297
Peptide name
Tumor protein p73
Ligandability
Cysteine 295 of Tumor protein p73
Cysteine 297 of Tumor protein p73
3vd2 I 153 I 295
A redox-regulated disulphide may form within Tumor protein p73 between cysteines 153 and 295. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
3vd2
Structure name
structure of p73 dna binding domain tetramer modulates p73 transactivation
Structure deposition date
2012-01-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
9
% buried
99
Peptide accession
O15350
Residue number A
153
Residue number B
295
Peptide name
Tumor protein p73
Ligandability
Cysteine 153 of Tumor protein p73
Cysteine 295 of Tumor protein p73
3vd0 D 159 D 295
A redox-regulated disulphide may form within Tumor protein p73 between cysteines 159 and 295. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
3vd0
Structure name
structure of p73 dna binding domain tetramer modulates p73 transactivation
Structure deposition date
2012-01-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
9
% buried
100
Peptide accession
O15350
Residue number A
159
Residue number B
295
Peptide name
Tumor protein p73
Ligandability
Cysteine 159 of Tumor protein p73
Cysteine 295 of Tumor protein p73
6fgs A 74 A 84
A redox-regulated disulphide may form within Tumor protein p73 between cysteines 74 and 619 (74 and 84 respectively in this structure).
Details
Redox score ?
nan
PDB code
6fgs
Structure name
solution structure of p300taz2-p73ta1
Structure deposition date
2018-01-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
12
Peptide accession
O15350
Residue number A
74
Residue number B
619
Peptide name
Tumor protein p73
Ligandability
Cysteine 74 of Tumor protein p73
Cysteine 619 of Tumor protein p73
Cysteine 74 in protein A could not be asigned to a Uniprot residue.
6fgs A 74 A 79
A redox-regulated disulphide may form within Tumor protein p73 between cysteines 74 and 79.
Details
Redox score ?
nan
PDB code
6fgs
Structure name
solution structure of p300taz2-p73ta1
Structure deposition date
2018-01-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
2
Peptide accession
O15350
Residue number A
74
Residue number B
79
Peptide name
Tumor protein p73
Ligandability
Cysteine 74 of Tumor protein p73
Cysteine 79 of Tumor protein p73
Cysteine 74 in protein A could not be asigned to a Uniprot residue.
Cysteine 79 in protein B could not be asigned to a Uniprot residue.
6fgs A 26 A 31
A redox-regulated disulphide may form within Tumor protein p73 between cysteines 26 and 31.
Details
Redox score ?
nan
PDB code
6fgs
Structure name
solution structure of p300taz2-p73ta1
Structure deposition date
2018-01-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
7
% buried
0
Peptide accession
O15350
Residue number A
26
Residue number B
31
Peptide name
Tumor protein p73
Ligandability
Cysteine 26 of Tumor protein p73
Cysteine 31 of Tumor protein p73
Cysteine 26 in protein A could not be asigned to a Uniprot residue.
Cysteine 31 in protein B could not be asigned to a Uniprot residue.
6fgs A 49 A 57
A redox-regulated disulphide may form within Tumor protein p73 between cysteines 49 and 502 (49 and 57 respectively in this structure).
Details
Redox score ?
nan
PDB code
6fgs
Structure name
solution structure of p300taz2-p73ta1
Structure deposition date
2018-01-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
40
Minimum pKa ?
7
% buried
2
Peptide accession
O15350
Residue number A
49
Residue number B
502
Peptide name
Tumor protein p73
Ligandability
Cysteine 49 of Tumor protein p73
Cysteine 502 of Tumor protein p73
Cysteine 49 in protein A could not be asigned to a Uniprot residue.
6fgs A 49 A 60
A redox-regulated disulphide may form within Tumor protein p73 between cysteines 49 and 505 (49 and 60 respectively in this structure).
Details
Redox score ?
nan
PDB code
6fgs
Structure name
solution structure of p300taz2-p73ta1
Structure deposition date
2018-01-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
6
Peptide accession
O15350
Residue number A
49
Residue number B
505
Peptide name
Tumor protein p73
Ligandability
Cysteine 49 of Tumor protein p73
Cysteine 505 of Tumor protein p73
Cysteine 49 in protein A could not be asigned to a Uniprot residue.
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