Tumor protein 63
Intermolecular
Cysteine 244 and cysteine 244
Intramolecular
Cysteine 308 and cysteine 312
Cysteine 244 and cysteine 312
Cysteine 244 and cysteine 308
Cysteine 203 and cysteine 209
Cysteine 558 and cysteine 561
Cysteine 345 and cysteine 347
Cysteine 203 and cysteine 345
Cysteine 14 and cysteine 84
Cysteine 26 and cysteine 36
More...Cysteine 26 and cysteine 31
Cysteine 57 and cysteine 60
Cysteine 49 and cysteine 57
Cysteine 49 and cysteine 60
3qym C 205 D 205
A redox-regulated disulphide may form between two units of Tumor protein 63 at cysteines 244 and 244 (205 and 205 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
3qym
Structure name
structure of p63 dna binding domain in complex with a 10 base pair a/t rich response element half site
Structure deposition date
2011-03-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide A name
Tumor protein 63
Peptide B name
Tumor protein 63
Peptide A accession
Q9H3D4
Peptide B accession
Q9H3D4
Peptide A residue number
244
Peptide B residue number
244
Ligandability
3us2 A 269 A 273
A redox-regulated disulphide may form within Tumor protein 63 between cysteines 308 and 312 (269 and 273 respectively in this structure).
Details
Redox score ?
88
PDB code
3us2
Structure name
structure of p63 dna binding domain in complex with a 19 base pair a/t rich response element containing two half sites with a single base pair overlap
Structure deposition date
2011-11-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
1
% buried
96
Peptide accession
Q9H3D4
Residue number A
308
Residue number B
312
Peptide name
Tumor protein 63
Ligandability
Cysteine 308 of Tumor protein 63
Cysteine 312 of Tumor protein 63
2rmn A 205 A 273
A redox-regulated disulphide may form within Tumor protein 63 between cysteines 244 and 312 (205 and 273 respectively in this structure).
Details
Redox score ?
87
PDB code
2rmn
Structure name
the solution structure of the p63 dna-binding domain
Structure deposition date
2007-11-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
46
Minimum pKa ?
7
% buried
22
Peptide accession
Q9H3D4
Residue number A
244
Residue number B
312
Peptide name
Tumor protein 63
Ligandability
Cysteine 244 of Tumor protein 63
Cysteine 312 of Tumor protein 63
3us0 D 205 D 269
A redox-regulated disulphide may form within Tumor protein 63 between cysteines 244 and 308 (205 and 269 respectively in this structure).
Details
Redox score ?
75
PDB code
3us0
Structure name
structure of p63 dna binding domain in complex with a 22 base pair a/t rich response element containing a two base pair "at" spacer between half sites
Structure deposition date
2011-11-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
8
% buried
nan
Peptide accession
Q9H3D4
Residue number A
244
Residue number B
308
Peptide name
Tumor protein 63
Ligandability
Cysteine 244 of Tumor protein 63
Cysteine 308 of Tumor protein 63
3us2 B 164 B 170
A redox-regulated disulphide may form within Tumor protein 63 between cysteines 203 and 209 (164 and 170 respectively in this structure).
Details
Redox score ?
73
PDB code
3us2
Structure name
structure of p63 dna binding domain in complex with a 19 base pair a/t rich response element containing two half sites with a single base pair overlap
Structure deposition date
2011-11-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
70
Minimum pKa ?
9
% buried
100
Peptide accession
Q9H3D4
Residue number A
203
Residue number B
209
Peptide name
Tumor protein 63
Ligandability
Cysteine 203 of Tumor protein 63
Cysteine 209 of Tumor protein 63
1rg6 A 19 A 22
A redox-regulated disulphide may form within Tumor protein 63 between cysteines 558 and 561 (19 and 22 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
1rg6
Structure name
solution structure of the c-terminal domain of p63
Structure deposition date
2003-11-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
46
Minimum pKa ?
10
% buried
8
Peptide accession
Q9H3D4
Residue number A
558
Residue number B
561
Peptide name
Tumor protein 63
Ligandability
Cysteine 558 of Tumor protein 63
Cysteine 561 of Tumor protein 63
3qym F 306 F 308
A redox-regulated disulphide may form within Tumor protein 63 between cysteines 345 and 347 (306 and 308 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
3qym
Structure name
structure of p63 dna binding domain in complex with a 10 base pair a/t rich response element half site
Structure deposition date
2011-03-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
11
% buried
86
Peptide accession
Q9H3D4
Residue number A
345
Residue number B
347
Peptide name
Tumor protein 63
Ligandability
Cysteine 345 of Tumor protein 63
Cysteine 347 of Tumor protein 63
3qyn A 164 A 306
A redox-regulated disulphide may form within Tumor protein 63 between cysteines 203 and 345 (164 and 306 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
3qyn
Structure name
structure of p63 dna binding domain in complex with a 22 base pair a/t rich response element containing 2 base pair spacer between half sites
Structure deposition date
2011-03-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
15
% buried
98
Peptide accession
Q9H3D4
Residue number A
203
Residue number B
345
Peptide name
Tumor protein 63
Ligandability
Cysteine 203 of Tumor protein 63
Cysteine 345 of Tumor protein 63
6fgn A 79 A 84
A redox-regulated disulphide may form within Tumor protein 63 between cysteines 14 and 84 (79 and 84 respectively in this structure).
Details
Redox score ?
nan
PDB code
6fgn
Structure name
solution structure of p300taz2-p63ta
Structure deposition date
2018-01-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
58
Minimum pKa ?
7
% buried
20
Peptide accession
Q9H3D4
Residue number A
14
Residue number B
84
Peptide name
Tumor protein 63
Ligandability
Cysteine 14 of Tumor protein 63
Cysteine 84 of Tumor protein 63
Uncertain whether structure cysteine 79 has been assigned to correct residue.
Cysteine 84 in protein B could not be asigned to a Uniprot residue.
6fgn A 26 A 36
A redox-regulated disulphide may form within Tumor protein 63 between cysteines 26 and 36.
Details
Redox score ?
nan
PDB code
6fgn
Structure name
solution structure of p300taz2-p63ta
Structure deposition date
2018-01-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
52
Minimum pKa ?
6
% buried
0
Peptide accession
Q9H3D4
Residue number A
26
Residue number B
36
Peptide name
Tumor protein 63
Ligandability
Cysteine 26 of Tumor protein 63
Cysteine 36 of Tumor protein 63
Cysteine 26 in protein A could not be asigned to a Uniprot residue.
Cysteine 36 in protein B could not be asigned to a Uniprot residue.
6fgn A 26 A 31
A redox-regulated disulphide may form within Tumor protein 63 between cysteines 26 and 31.
Details
Redox score ?
nan
PDB code
6fgn
Structure name
solution structure of p300taz2-p63ta
Structure deposition date
2018-01-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
39
Minimum pKa ?
6
% buried
0
Peptide accession
Q9H3D4
Residue number A
26
Residue number B
31
Peptide name
Tumor protein 63
Ligandability
Cysteine 26 of Tumor protein 63
Cysteine 31 of Tumor protein 63
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.
6fgn A 57 A 60
A redox-regulated disulphide may form within Tumor protein 63 between cysteines 57 and 60.
Details
Redox score ?
nan
PDB code
6fgn
Structure name
solution structure of p300taz2-p63ta
Structure deposition date
2018-01-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
24
Peptide accession
Q9H3D4
Residue number A
57
Residue number B
60
Peptide name
Tumor protein 63
Ligandability
Cysteine 57 of Tumor protein 63
Cysteine 60 of Tumor protein 63
Cysteine 57 in protein A could not be asigned to a Uniprot residue.
Cysteine 60 in protein B could not be asigned to a Uniprot residue.
6fgn A 49 A 57
A redox-regulated disulphide may form within Tumor protein 63 between cysteines 49 and 57.
Details
Redox score ?
nan
PDB code
6fgn
Structure name
solution structure of p300taz2-p63ta
Structure deposition date
2018-01-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
8
Peptide accession
Q9H3D4
Residue number A
49
Residue number B
57
Peptide name
Tumor protein 63
Ligandability
Cysteine 49 of Tumor protein 63
Cysteine 57 of Tumor protein 63
Cysteine 49 in protein A could not be asigned to a Uniprot residue.
Cysteine 57 in protein B could not be asigned to a Uniprot residue.
6fgn A 49 A 60
A redox-regulated disulphide may form within Tumor protein 63 between cysteines 49 and 60.
Details
Redox score ?
nan
PDB code
6fgn
Structure name
solution structure of p300taz2-p63ta
Structure deposition date
2018-01-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
16
Peptide accession
Q9H3D4
Residue number A
49
Residue number B
60
Peptide name
Tumor protein 63
Ligandability
Cysteine 49 of Tumor protein 63
Cysteine 60 of Tumor protein 63
Cysteine 49 in protein A could not be asigned to a Uniprot residue.
Cysteine 60 in protein B could not be asigned to a Uniprot residue.
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