DNA topoisomerase 2-binding protein 1
Intermolecular
Cysteine 1299 and cysteine 844 of Histone lysine demethylase PHF8
Intramolecular
Cysteine 206 and cysteine 238
Cysteine 203 and cysteine 276
Cysteine 87 and cysteine 93
Cysteine 1463 and cysteine 1485
Cysteine 203 and cysteine 238
Cysteine 197 and cysteine 203
Cysteine 238 and cysteine 261
Cysteine 977 and cysteine 981
Cysteine 238 and cysteine 253
More...Cysteine 60 and cysteine 76
Cysteine 253 and cysteine 261
Cysteine 362 and cysteine 430
Cysteine 206 and cysteine 261
Cysteine 206 and cysteine 253
Cysteine 197 and cysteine 276
7cmz A 1299 B 844
A redox-regulated disulphide may form between cysteine 1299 of DNA topoisomerase 2-binding protein 1 and cysteine 844 of Histone lysine demethylase PHF8.
Details
Redox score ?
86
PDB code
7cmz
Structure name
crystal structure of brct7/8 in complex with the aps motif of phf8
Structure deposition date
2020-07-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide A name
DNA topoisomerase 2-binding protein 1
Peptide B name
Histone lysine demethylase PHF8
Peptide A accession
Q92547
Peptide B accession
Q9UPP1
Peptide A residue number
1299
Peptide B residue number
844
Ligandability
Cysteine 1299 of DNA topoisomerase 2-binding protein 1
Cysteine 844 of Histone lysine demethylase PHF8
6rml A 206 A 238
A redox-regulated disulphide may form within DNA topoisomerase 2-binding protein 1 between cysteines 206 and 238.
Details
Redox score ?
74
PDB code
6rml
Structure name
crystal structure of topbp1 brct0,1,2 in complex with a 53bp1 phosphopeptide
Structure deposition date
2019-05-07
Thiol separation (Å)
3
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
46
Peptide accession
Q92547
Residue number A
206
Residue number B
238
Peptide name
DNA topoisomerase 2-binding protein 1
Ligandability
Cysteine 206 of DNA topoisomerase 2-binding protein 1
Cysteine 238 of DNA topoisomerase 2-binding protein 1
2xnk D 203 D 276
A redox-regulated disulphide may form within DNA topoisomerase 2-binding protein 1 between cysteines 203 and 276.
Details
Redox score ?
73
PDB code
2xnk
Structure name
structure and function of the rad9-binding region of the dna damage checkpoint adaptor topbp1
Structure deposition date
2010-08-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
6
% buried
94
Peptide accession
Q92547
Residue number A
203
Residue number B
276
Peptide name
DNA topoisomerase 2-binding protein 1
Ligandability
Cysteine 203 of DNA topoisomerase 2-binding protein 1
Cysteine 276 of DNA topoisomerase 2-binding protein 1
2xnk A 87 A 93
A redox-regulated disulphide may form within DNA topoisomerase 2-binding protein 1 between cysteines 87 and 93.
Details
Redox score ?
61
PDB code
2xnk
Structure name
structure and function of the rad9-binding region of the dna damage checkpoint adaptor topbp1
Structure deposition date
2010-08-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
46
Peptide accession
Q92547
Residue number A
87
Residue number B
93
Peptide name
DNA topoisomerase 2-binding protein 1
Ligandability
Cysteine 87 of DNA topoisomerase 2-binding protein 1
Cysteine 93 of DNA topoisomerase 2-binding protein 1
3al3 A 1463 A 1485
A redox-regulated disulphide may form within DNA topoisomerase 2-binding protein 1 between cysteines 1463 and 1485. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
3al3
Structure name
crystal structure of topbp1 brct7/8-bach1 peptide complex
Structure deposition date
2010-07-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
30
Peptide accession
Q92547
Residue number A
1463
Residue number B
1485
Peptide name
DNA topoisomerase 2-binding protein 1
Ligandability
Cysteine 1463 of DNA topoisomerase 2-binding protein 1
Cysteine 1485 of DNA topoisomerase 2-binding protein 1
2xnk A 203 A 238
A redox-regulated disulphide may form within DNA topoisomerase 2-binding protein 1 between cysteines 203 and 238. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
2xnk
Structure name
structure and function of the rad9-binding region of the dna damage checkpoint adaptor topbp1
Structure deposition date
2010-08-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
5
% buried
87
Peptide accession
Q92547
Residue number A
203
Residue number B
238
Peptide name
DNA topoisomerase 2-binding protein 1
Ligandability
Cysteine 203 of DNA topoisomerase 2-binding protein 1
Cysteine 238 of DNA topoisomerase 2-binding protein 1
2xnk A 197 A 203
A redox-regulated disulphide may form within DNA topoisomerase 2-binding protein 1 between cysteines 197 and 203. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
2xnk
Structure name
structure and function of the rad9-binding region of the dna damage checkpoint adaptor topbp1
Structure deposition date
2010-08-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
5
% buried
84
Peptide accession
Q92547
Residue number A
197
Residue number B
203
Peptide name
DNA topoisomerase 2-binding protein 1
Ligandability
Cysteine 197 of DNA topoisomerase 2-binding protein 1
Cysteine 203 of DNA topoisomerase 2-binding protein 1
6rml B 238 B 261
A redox-regulated disulphide may form within DNA topoisomerase 2-binding protein 1 between cysteines 238 and 261. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
6rml
Structure name
crystal structure of topbp1 brct0,1,2 in complex with a 53bp1 phosphopeptide
Structure deposition date
2019-05-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
58
Peptide accession
Q92547
Residue number A
238
Residue number B
261
Peptide name
DNA topoisomerase 2-binding protein 1
Ligandability
Cysteine 238 of DNA topoisomerase 2-binding protein 1
Cysteine 261 of DNA topoisomerase 2-binding protein 1
3pd7 B 977 B 981
A redox-regulated disulphide may form within DNA topoisomerase 2-binding protein 1 between cysteines 977 and 981. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
3pd7
Structure name
crystal structure of the sixth brct domain of human topbp1
Structure deposition date
2010-10-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
22
Peptide accession
Q92547
Residue number A
977
Residue number B
981
Peptide name
DNA topoisomerase 2-binding protein 1
Ligandability
Cysteine 977 of DNA topoisomerase 2-binding protein 1
Cysteine 981 of DNA topoisomerase 2-binding protein 1
3olc X 238 X 253
A redox-regulated disulphide may form within DNA topoisomerase 2-binding protein 1 between cysteines 238 and 253. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
3olc
Structure name
crystal structure of the n-terminal region of topbp1
Structure deposition date
2010-08-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
29
Peptide accession
Q92547
Residue number A
238
Residue number B
253
Peptide name
DNA topoisomerase 2-binding protein 1
Ligandability
Cysteine 238 of DNA topoisomerase 2-binding protein 1
Cysteine 253 of DNA topoisomerase 2-binding protein 1
2xnk D 60 D 76
A redox-regulated disulphide may form within DNA topoisomerase 2-binding protein 1 between cysteines 60 and 76. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
2xnk
Structure name
structure and function of the rad9-binding region of the dna damage checkpoint adaptor topbp1
Structure deposition date
2010-08-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
68
Peptide accession
Q92547
Residue number A
60
Residue number B
76
Peptide name
DNA topoisomerase 2-binding protein 1
Ligandability
Cysteine 60 of DNA topoisomerase 2-binding protein 1
Cysteine 76 of DNA topoisomerase 2-binding protein 1
6rml B 253 B 261
A redox-regulated disulphide may form within DNA topoisomerase 2-binding protein 1 between cysteines 253 and 261. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
6rml
Structure name
crystal structure of topbp1 brct0,1,2 in complex with a 53bp1 phosphopeptide
Structure deposition date
2019-05-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
29
Peptide accession
Q92547
Residue number A
253
Residue number B
261
Peptide name
DNA topoisomerase 2-binding protein 1
Ligandability
Cysteine 253 of DNA topoisomerase 2-binding protein 1
Cysteine 261 of DNA topoisomerase 2-binding protein 1
1wf6 A 44 A 112
A redox-regulated disulphide may form within DNA topoisomerase 2-binding protein 1 between cysteines 362 and 430 (44 and 112 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
1wf6
Structure name
the third brca1 c-terminus (brct) domain of similar to s
Structure deposition date
2004-05-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
50
Peptide accession
Q92547
Residue number A
362
Residue number B
430
Peptide name
DNA topoisomerase 2-binding protein 1
Ligandability
Cysteine 362 of DNA topoisomerase 2-binding protein 1
Cysteine 430 of DNA topoisomerase 2-binding protein 1
2xnk B 206 B 261
A redox-regulated disulphide may form within DNA topoisomerase 2-binding protein 1 between cysteines 206 and 261. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
2xnk
Structure name
structure and function of the rad9-binding region of the dna damage checkpoint adaptor topbp1
Structure deposition date
2010-08-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
nan
Peptide accession
Q92547
Residue number A
206
Residue number B
261
Peptide name
DNA topoisomerase 2-binding protein 1
Ligandability
Cysteine 206 of DNA topoisomerase 2-binding protein 1
Cysteine 261 of DNA topoisomerase 2-binding protein 1
6rml B 206 B 253
A redox-regulated disulphide may form within DNA topoisomerase 2-binding protein 1 between cysteines 206 and 253. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
6rml
Structure name
crystal structure of topbp1 brct0,1,2 in complex with a 53bp1 phosphopeptide
Structure deposition date
2019-05-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
46
Peptide accession
Q92547
Residue number A
206
Residue number B
253
Peptide name
DNA topoisomerase 2-binding protein 1
Ligandability
Cysteine 206 of DNA topoisomerase 2-binding protein 1
Cysteine 253 of DNA topoisomerase 2-binding protein 1
2xnk C 197 C 276
A redox-regulated disulphide may form within DNA topoisomerase 2-binding protein 1 between cysteines 197 and 276. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
2xnk
Structure name
structure and function of the rad9-binding region of the dna damage checkpoint adaptor topbp1
Structure deposition date
2010-08-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
86
Peptide accession
Q92547
Residue number A
197
Residue number B
276
Peptide name
DNA topoisomerase 2-binding protein 1
Ligandability
Cysteine 197 of DNA topoisomerase 2-binding protein 1
Cysteine 276 of DNA topoisomerase 2-binding protein 1
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