Death-inducer obliterator 1
Intramolecular
Cysteine 282 and cysteine 313
Cysteine 282 and cysteine 316
Cysteine 285 and cysteine 288
Cysteine 271 and cysteine 296
Cysteine 268 and cysteine 270
Cysteine 313 and cysteine 316
Cysteine 285 and cysteine 316
Cysteine 273 and cysteine 296
Cysteine 285 and cysteine 313
Cysteine 284 and cysteine 285
More...Cysteine 268 and cysteine 313
Cysteine 284 and cysteine 288
Cysteine 268 and cysteine 285
Cysteine 284 and cysteine 316
1wem A 33 A 64
A redox-regulated disulphide may form within Death-inducer obliterator 1 between cysteines 282 and 313 (33 and 64 respectively in this structure).
Details
Redox score ?
88
PDB code
1wem
Structure name
solution structure of phd domain in death inducer-obliterator 1(dio-1)
Structure deposition date
2004-05-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
5
% buried
12
Peptide accession
Q8C9B9
Residue number A
282
Residue number B
313
Peptide name
Death-inducer obliterator 1
Ligandability
Cysteine 282 of Death-inducer obliterator 1
Cysteine 313 of Death-inducer obliterator 1
1wem A 33 A 67
A redox-regulated disulphide may form within Death-inducer obliterator 1 between cysteines 282 and 316 (33 and 67 respectively in this structure).
Details
Redox score ?
88
PDB code
1wem
Structure name
solution structure of phd domain in death inducer-obliterator 1(dio-1)
Structure deposition date
2004-05-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
5
% buried
6
Peptide accession
Q8C9B9
Residue number A
282
Residue number B
316
Peptide name
Death-inducer obliterator 1
Ligandability
Cysteine 282 of Death-inducer obliterator 1
Cysteine 316 of Death-inducer obliterator 1
4l7x A 23 A 26
A redox-regulated disulphide may form within Death-inducer obliterator 1 between cysteines 285 and 288 (23 and 26 respectively in this structure).
Details
Redox score ?
86
PDB code
4l7x
Structure name
crystal structure of the dido phd finger in complex with h3k4me3
Structure deposition date
2013-06-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
4
Peptide accession
Q9BTC0
Residue number A
285
Residue number B
288
Peptide name
Death-inducer obliterator 1
Ligandability
Cysteine 285 of Death-inducer obliterator 1
Cysteine 288 of Death-inducer obliterator 1
4l7x A 9 A 34
A redox-regulated disulphide may form within Death-inducer obliterator 1 between cysteines 271 and 296 (9 and 34 respectively in this structure).
Details
Redox score ?
86
PDB code
4l7x
Structure name
crystal structure of the dido phd finger in complex with h3k4me3
Structure deposition date
2013-06-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
16
Peptide accession
Q9BTC0
Residue number A
271
Residue number B
296
Peptide name
Death-inducer obliterator 1
Ligandability
Cysteine 271 of Death-inducer obliterator 1
Cysteine 296 of Death-inducer obliterator 1
1wem A 19 A 21
A redox-regulated disulphide may form within Death-inducer obliterator 1 between cysteines 268 and 270 (19 and 21 respectively in this structure).
Details
Redox score ?
86
PDB code
1wem
Structure name
solution structure of phd domain in death inducer-obliterator 1(dio-1)
Structure deposition date
2004-05-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
6
% buried
10
Peptide accession
Q8C9B9
Residue number A
268
Residue number B
270
Peptide name
Death-inducer obliterator 1
Ligandability
Cysteine 268 of Death-inducer obliterator 1
Cysteine 270 of Death-inducer obliterator 1
1wem A 64 A 67
A redox-regulated disulphide may form within Death-inducer obliterator 1 between cysteines 313 and 316 (64 and 67 respectively in this structure).
Details
Redox score ?
84
PDB code
1wem
Structure name
solution structure of phd domain in death inducer-obliterator 1(dio-1)
Structure deposition date
2004-05-25
Thiol separation (Å)
3
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
6
Peptide accession
Q8C9B9
Residue number A
313
Residue number B
316
Peptide name
Death-inducer obliterator 1
Ligandability
Cysteine 313 of Death-inducer obliterator 1
Cysteine 316 of Death-inducer obliterator 1
1wem A 36 A 67
A redox-regulated disulphide may form within Death-inducer obliterator 1 between cysteines 285 and 316 (36 and 67 respectively in this structure).
Details
Redox score ?
83
PDB code
1wem
Structure name
solution structure of phd domain in death inducer-obliterator 1(dio-1)
Structure deposition date
2004-05-25
Thiol separation (Å)
3
Half-sphere exposure sum ?
42
Minimum pKa ?
9
% buried
2
Peptide accession
Q8C9B9
Residue number A
285
Residue number B
316
Peptide name
Death-inducer obliterator 1
Ligandability
Cysteine 285 of Death-inducer obliterator 1
Cysteine 316 of Death-inducer obliterator 1
4l7x A 11 A 34
A redox-regulated disulphide may form within Death-inducer obliterator 1 between cysteines 273 and 296 (11 and 34 respectively in this structure).
Details
Redox score ?
78
PDB code
4l7x
Structure name
crystal structure of the dido phd finger in complex with h3k4me3
Structure deposition date
2013-06-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
9
% buried
4
Peptide accession
Q9BTC0
Residue number A
273
Residue number B
296
Peptide name
Death-inducer obliterator 1
Ligandability
Cysteine 273 of Death-inducer obliterator 1
Cysteine 296 of Death-inducer obliterator 1
1wem A 36 A 64
A redox-regulated disulphide may form within Death-inducer obliterator 1 between cysteines 285 and 313 (36 and 64 respectively in this structure).
Details
Redox score ?
75
PDB code
1wem
Structure name
solution structure of phd domain in death inducer-obliterator 1(dio-1)
Structure deposition date
2004-05-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
11
% buried
8
Peptide accession
Q8C9B9
Residue number A
285
Residue number B
313
Peptide name
Death-inducer obliterator 1
Ligandability
Cysteine 285 of Death-inducer obliterator 1
Cysteine 313 of Death-inducer obliterator 1
4l7x A 22 A 23
A redox-regulated disulphide may form within Death-inducer obliterator 1 between cysteines 284 and 285 (22 and 23 respectively in this structure).
Details
Redox score ?
63
PDB code
4l7x
Structure name
crystal structure of the dido phd finger in complex with h3k4me3
Structure deposition date
2013-06-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
6
% buried
18
Peptide accession
Q9BTC0
Residue number A
284
Residue number B
285
Peptide name
Death-inducer obliterator 1
Ligandability
Cysteine 284 of Death-inducer obliterator 1
Cysteine 285 of Death-inducer obliterator 1
1wem A 19 A 64
A redox-regulated disulphide may form within Death-inducer obliterator 1 between cysteines 268 and 313 (19 and 64 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
1wem
Structure name
solution structure of phd domain in death inducer-obliterator 1(dio-1)
Structure deposition date
2004-05-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
6
% buried
15
Peptide accession
Q8C9B9
Residue number A
268
Residue number B
313
Peptide name
Death-inducer obliterator 1
Ligandability
Cysteine 268 of Death-inducer obliterator 1
Cysteine 313 of Death-inducer obliterator 1
4l7x A 22 A 26
A redox-regulated disulphide may form within Death-inducer obliterator 1 between cysteines 284 and 288 (22 and 26 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
4l7x
Structure name
crystal structure of the dido phd finger in complex with h3k4me3
Structure deposition date
2013-06-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
14
Peptide accession
Q9BTC0
Residue number A
284
Residue number B
288
Peptide name
Death-inducer obliterator 1
Ligandability
Cysteine 284 of Death-inducer obliterator 1
Cysteine 288 of Death-inducer obliterator 1
1wem A 19 A 36
A redox-regulated disulphide may form within Death-inducer obliterator 1 between cysteines 268 and 285 (19 and 36 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
1wem
Structure name
solution structure of phd domain in death inducer-obliterator 1(dio-1)
Structure deposition date
2004-05-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
10
Peptide accession
Q8C9B9
Residue number A
268
Residue number B
285
Peptide name
Death-inducer obliterator 1
Ligandability
Cysteine 268 of Death-inducer obliterator 1
Cysteine 285 of Death-inducer obliterator 1
4l7x A 22 A 54
A redox-regulated disulphide may form within Death-inducer obliterator 1 between cysteines 284 and 316 (22 and 54 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
4l7x
Structure name
crystal structure of the dido phd finger in complex with h3k4me3
Structure deposition date
2013-06-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
15
Peptide accession
Q9BTC0
Residue number A
284
Residue number B
316
Peptide name
Death-inducer obliterator 1
Ligandability
Cysteine 284 of Death-inducer obliterator 1
Cysteine 316 of Death-inducer obliterator 1
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