Tyrosyl-DNA phosphodiesterase 2
Intermolecular
Cysteine 137 and cysteine 137
Cysteine 137 and cysteine 352
Cysteine 137 and cysteine 147
Cysteine 311 and cysteine 137
Intramolecular
Cysteine 210 and cysteine 221
Cysteine 29 and cysteine 38
Cysteine 29 and cysteine 45
Cysteine 293 and cysteine 356
Cysteine 147 and cysteine 149
Cysteine 38 and cysteine 45
5j3z A 137 B 137
A redox-regulated disulphide may form between two units of Tyrosyl-DNA phosphodiesterase 2 at cysteines 137 and 137.
Details
Redox score ?
84
PDB code
5j3z
Structure name
crystal structure of m2htdp2-cat in complex with a small molecule inhibitor
Structure deposition date
2016-03-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide A name
Tyrosyl-DNA phosphodiesterase 2
Peptide B name
Tyrosyl-DNA phosphodiesterase 2
Peptide A accession
Q9JJX7
Peptide B accession
Q9JJX7
Peptide A residue number
137
Peptide B residue number
137
Ligandability
5j3z A 137 B 352
A redox-regulated disulphide may form between two units of Tyrosyl-DNA phosphodiesterase 2 at cysteines 137 and 352. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
5j3z
Structure name
crystal structure of m2htdp2-cat in complex with a small molecule inhibitor
Structure deposition date
2016-03-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
11
% buried
nan
Peptide A name
Tyrosyl-DNA phosphodiesterase 2
Peptide B name
Tyrosyl-DNA phosphodiesterase 2
Peptide A accession
Q9JJX7
Peptide B accession
Q9JJX7
Peptide A residue number
137
Peptide B residue number
352
Ligandability
Cysteine 137 of Tyrosyl-DNA phosphodiesterase 2
Cysteine 352 of Tyrosyl-DNA phosphodiesterase 2
4gyz A 137 B 147
A redox-regulated disulphide may form between two units of Tyrosyl-DNA phosphodiesterase 2 at cysteines 137 and 147. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
4gyz
Structure name
mus musculus tdp2 bound to damp and mg2+
Structure deposition date
2012-09-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
74
Peptide A name
Tyrosyl-DNA phosphodiesterase 2
Peptide B name
Tyrosyl-DNA phosphodiesterase 2
Peptide A accession
Q9JJX7
Peptide B accession
Q9JJX7
Peptide A residue number
137
Peptide B residue number
147
Ligandability
Cysteine 137 of Tyrosyl-DNA phosphodiesterase 2
Cysteine 147 of Tyrosyl-DNA phosphodiesterase 2
5j3p A 311 B 137
A redox-regulated disulphide may form between two units of Tyrosyl-DNA phosphodiesterase 2 at cysteines 311 and 137. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
5j3p
Structure name
crystal structure of the catalytic domain of human tyrosyl dna phosphodiesterase 2
Structure deposition date
2016-03-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
74
Peptide A name
Tyrosyl-DNA phosphodiesterase 2
Peptide B name
Tyrosyl-DNA phosphodiesterase 2
Peptide A accession
O95551
Peptide B accession
O95551
Peptide A residue number
311
Peptide B residue number
137
Ligandability
Cysteine 311 of Tyrosyl-DNA phosphodiesterase 2
Cysteine 137 of Tyrosyl-DNA phosphodiesterase 2
5j3s A 210 A 221
A redox-regulated disulphide may form within Tyrosyl-DNA phosphodiesterase 2 between cysteines 210 and 221.
Details
Redox score ?
72
PDB code
5j3s
Structure name
crystal structure of the catalytic domain of human tyrosyl dna phosphodiesterase 2 in complex with a small molecule inhibitor
Structure deposition date
2016-03-31
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
7
% buried
48
Peptide accession
O95551
Residue number A
210
Residue number B
221
Peptide name
Tyrosyl-DNA phosphodiesterase 2
Ligandability
Cysteine 210 of Tyrosyl-DNA phosphodiesterase 2
Cysteine 221 of Tyrosyl-DNA phosphodiesterase 2
6q01 C 29 C 38
A redox-regulated disulphide may form within Tyrosyl-DNA phosphodiesterase 2 between cysteines 29 and 38. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
6q01
Structure name
tdp2 uba domain bound to ubiquitin at 0
Structure deposition date
2019-08-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
18
Peptide accession
O95551
Residue number A
29
Residue number B
38
Peptide name
Tyrosyl-DNA phosphodiesterase 2
Ligandability
Cysteine 29 of Tyrosyl-DNA phosphodiesterase 2
Cysteine 38 of Tyrosyl-DNA phosphodiesterase 2
6q01 C 29 C 45
A redox-regulated disulphide may form within Tyrosyl-DNA phosphodiesterase 2 between cysteines 29 and 45. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
6q01
Structure name
tdp2 uba domain bound to ubiquitin at 0
Structure deposition date
2019-08-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
7
Peptide accession
O95551
Residue number A
29
Residue number B
45
Peptide name
Tyrosyl-DNA phosphodiesterase 2
Ligandability
Cysteine 29 of Tyrosyl-DNA phosphodiesterase 2
Cysteine 45 of Tyrosyl-DNA phosphodiesterase 2
5ino A 293 A 356
A redox-regulated disulphide may form within Tyrosyl-DNA phosphodiesterase 2 between cysteines 293 and 356. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
5ino
Structure name
human tdp2 reaction product (5'-phosphorylated dna)-mg2+ complex
Structure deposition date
2016-03-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
74
Peptide accession
O95551
Residue number A
293
Residue number B
356
Peptide name
Tyrosyl-DNA phosphodiesterase 2
Ligandability
Cysteine 293 of Tyrosyl-DNA phosphodiesterase 2
Cysteine 356 of Tyrosyl-DNA phosphodiesterase 2
5inq B 147 B 149
A redox-regulated disulphide may form within Tyrosyl-DNA phosphodiesterase 2 between cysteines 147 and 149. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5inq
Structure name
mouse tdp2 reaction product (5'-phosphorylated dna)-ca2+ complex
Structure deposition date
2016-03-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
66
Peptide accession
Q9JJX7
Residue number A
147
Residue number B
149
Peptide name
Tyrosyl-DNA phosphodiesterase 2
Ligandability
Cysteine 147 of Tyrosyl-DNA phosphodiesterase 2
Cysteine 149 of Tyrosyl-DNA phosphodiesterase 2
6q01 D 38 D 45
A redox-regulated disulphide may form within Tyrosyl-DNA phosphodiesterase 2 between cysteines 38 and 45. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
6q01
Structure name
tdp2 uba domain bound to ubiquitin at 0
Structure deposition date
2019-08-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
76
Peptide accession
O95551
Residue number A
38
Residue number B
45
Peptide name
Tyrosyl-DNA phosphodiesterase 2
Ligandability
Cysteine 38 of Tyrosyl-DNA phosphodiesterase 2
Cysteine 45 of Tyrosyl-DNA phosphodiesterase 2
If this tool was useful for finding a disulphide, please cite: