Zinc finger protein ubi-d4
Intermolecular
Cysteine 486 of SWI/SNF complex subunit SMARCC2 and cysteine 24 L
Intramolecular
Cysteine 330 and cysteine 333
Cysteine 333 and cysteine 356
Cysteine 273 and cysteine 276
Cysteine 295 and cysteine 327
Cysteine 276 and cysteine 306
Cysteine 295 and cysteine 298
Cysteine 211 and cysteine 214
Cysteine 295 and cysteine 324
Cysteine 330 and cysteine 356
More...Cysteine 273 and cysteine 306
Cysteine 324 and cysteine 327
Cysteine 298 and cysteine 327
Cysteine 298 and cysteine 324
Cysteine 345 and cysteine 374
Cysteine 345 and cysteine 348
Cysteine 371 and cysteine 374
Cysteine 348 and cysteine 374
Cysteine 348 and cysteine 371
Cysteine 329 and cysteine 333
Cysteine 345 and cysteine 371
Cysteine 329 and cysteine 330
Cysteine 327 and cysteine 329
Cysteine 295 and cysteine 329
6ltj O 486 R 24
A redox-regulated disulphide may form between cysteine 486 of SWI/SNF complex subunit SMARCC2 and cysteine 24 of Zinc finger protein ubi-d4. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
6ltj
Structure name
structure of nucleosome-bound human baf complex
Structure deposition date
2020-01-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
90
Minimum pKa ?
12
% buried
100
Peptide A name
SWI/SNF complex subunit SMARCC2
Peptide B name
Zinc finger protein ubi-d4
Peptide A accession
Q8TAQ2
Peptide B accession
Q92785
Peptide A residue number
486
Peptide B residue number
24
Ligandability
Cysteine 486 of SWI/SNF complex subunit SMARCC2
Cysteine 24 of Zinc finger protein ubi-d4
5vdc A 61 A 64
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 330 and 333 (61 and 64 respectively in this structure).
Details
Redox score ?
86
PDB code
5vdc
Structure name
crystal structure of the human dpf2 tandem phd finger domain
Structure deposition date
2017-04-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
5
% buried
14
Peptide accession
Q92785
Residue number A
330
Residue number B
333
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 330 of Zinc finger protein ubi-d4
Cysteine 333 of Zinc finger protein ubi-d4
5b79 A 74 A 97
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 333 and 356 (74 and 97 respectively in this structure).
Details
Redox score ?
86
PDB code
5b79
Structure name
crystal structure of dpf2 double phd finger
Structure deposition date
2016-06-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
5
% buried
0
Peptide accession
Q92785
Residue number A
333
Residue number B
356
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 333 of Zinc finger protein ubi-d4
Cysteine 356 of Zinc finger protein ubi-d4
5b79 A 14 A 17
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 273 and 276 (14 and 17 respectively in this structure).
Details
Redox score ?
86
PDB code
5b79
Structure name
crystal structure of dpf2 double phd finger
Structure deposition date
2016-06-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
10
Peptide accession
Q92785
Residue number A
273
Residue number B
276
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 273 of Zinc finger protein ubi-d4
Cysteine 276 of Zinc finger protein ubi-d4
5vdc A 26 A 58
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 295 and 327 (26 and 58 respectively in this structure).
Details
Redox score ?
86
PDB code
5vdc
Structure name
crystal structure of the human dpf2 tandem phd finger domain
Structure deposition date
2017-04-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
5
% buried
10
Peptide accession
Q92785
Residue number A
295
Residue number B
327
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 295 of Zinc finger protein ubi-d4
Cysteine 327 of Zinc finger protein ubi-d4
5vdc A 7 A 37
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 276 and 306 (7 and 37 respectively in this structure).
Details
Redox score ?
85
PDB code
5vdc
Structure name
crystal structure of the human dpf2 tandem phd finger domain
Structure deposition date
2017-04-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
5
% buried
7
Peptide accession
Q92785
Residue number A
276
Residue number B
306
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 276 of Zinc finger protein ubi-d4
Cysteine 306 of Zinc finger protein ubi-d4
5vdc A 26 A 29
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 295 and 298 (26 and 29 respectively in this structure).
Details
Redox score ?
85
PDB code
5vdc
Structure name
crystal structure of the human dpf2 tandem phd finger domain
Structure deposition date
2017-04-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
5
% buried
10
Peptide accession
Q92785
Residue number A
295
Residue number B
298
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 295 of Zinc finger protein ubi-d4
Cysteine 298 of Zinc finger protein ubi-d4
3iuf A 211 A 214
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 211 and 214.
Details
Redox score ?
85
PDB code
3iuf
Structure name
crystal structure of the c2h2-type zinc finger domain of human ubi-d4
Structure deposition date
2009-08-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
7
% buried
0
Peptide accession
Q92785
Residue number A
211
Residue number B
214
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 211 of Zinc finger protein ubi-d4
Cysteine 214 of Zinc finger protein ubi-d4
5b79 A 36 A 65
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 295 and 324 (36 and 65 respectively in this structure).
Details
Redox score ?
83
PDB code
5b79
Structure name
crystal structure of dpf2 double phd finger
Structure deposition date
2016-06-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
5
% buried
18
Peptide accession
Q92785
Residue number A
295
Residue number B
324
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 295 of Zinc finger protein ubi-d4
Cysteine 324 of Zinc finger protein ubi-d4
5b79 A 71 A 97
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 330 and 356 (71 and 97 respectively in this structure).
Details
Redox score ?
83
PDB code
5b79
Structure name
crystal structure of dpf2 double phd finger
Structure deposition date
2016-06-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
7
% buried
12
Peptide accession
Q92785
Residue number A
330
Residue number B
356
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 330 of Zinc finger protein ubi-d4
Cysteine 356 of Zinc finger protein ubi-d4
5vdc A 4 A 37
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 273 and 306 (4 and 37 respectively in this structure).
Details
Redox score ?
82
PDB code
5vdc
Structure name
crystal structure of the human dpf2 tandem phd finger domain
Structure deposition date
2017-04-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
7
% buried
16
Peptide accession
Q92785
Residue number A
273
Residue number B
306
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 273 of Zinc finger protein ubi-d4
Cysteine 306 of Zinc finger protein ubi-d4
5b79 A 65 A 68
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 324 and 327 (65 and 68 respectively in this structure).
Details
Redox score ?
82
PDB code
5b79
Structure name
crystal structure of dpf2 double phd finger
Structure deposition date
2016-06-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
8
% buried
8
Peptide accession
Q92785
Residue number A
324
Residue number B
327
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 324 of Zinc finger protein ubi-d4
Cysteine 327 of Zinc finger protein ubi-d4
5b79 A 39 A 68
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 298 and 327 (39 and 68 respectively in this structure).
Details
Redox score ?
80
PDB code
5b79
Structure name
crystal structure of dpf2 double phd finger
Structure deposition date
2016-06-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
9
% buried
0
Peptide accession
Q92785
Residue number A
298
Residue number B
327
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 298 of Zinc finger protein ubi-d4
Cysteine 327 of Zinc finger protein ubi-d4
5b79 A 39 A 65
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 298 and 324 (39 and 65 respectively in this structure).
Details
Redox score ?
80
PDB code
5b79
Structure name
crystal structure of dpf2 double phd finger
Structure deposition date
2016-06-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
8
Peptide accession
Q92785
Residue number A
298
Residue number B
324
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 298 of Zinc finger protein ubi-d4
Cysteine 324 of Zinc finger protein ubi-d4
5b79 A 86 A 115
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 345 and 374 (86 and 115 respectively in this structure).
Details
Redox score ?
80
PDB code
5b79
Structure name
crystal structure of dpf2 double phd finger
Structure deposition date
2016-06-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
8
% buried
50
Peptide accession
Q92785
Residue number A
345
Residue number B
374
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 345 of Zinc finger protein ubi-d4
Cysteine 374 of Zinc finger protein ubi-d4
5b79 A 86 A 89
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 345 and 348 (86 and 89 respectively in this structure).
Details
Redox score ?
75
PDB code
5b79
Structure name
crystal structure of dpf2 double phd finger
Structure deposition date
2016-06-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
8
% buried
64
Peptide accession
Q92785
Residue number A
345
Residue number B
348
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 345 of Zinc finger protein ubi-d4
Cysteine 348 of Zinc finger protein ubi-d4
5vdc A 102 A 105
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 371 and 374 (102 and 105 respectively in this structure).
Details
Redox score ?
72
PDB code
5vdc
Structure name
crystal structure of the human dpf2 tandem phd finger domain
Structure deposition date
2017-04-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
11
% buried
nan
Peptide accession
Q92785
Residue number A
371
Residue number B
374
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 371 of Zinc finger protein ubi-d4
Cysteine 374 of Zinc finger protein ubi-d4
5b79 A 89 A 115
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 348 and 374 (89 and 115 respectively in this structure).
Details
Redox score ?
70
PDB code
5b79
Structure name
crystal structure of dpf2 double phd finger
Structure deposition date
2016-06-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
52
Peptide accession
Q92785
Residue number A
348
Residue number B
374
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 348 of Zinc finger protein ubi-d4
Cysteine 374 of Zinc finger protein ubi-d4
5vdc A 79 A 102
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 348 and 371 (79 and 102 respectively in this structure).
Details
Redox score ?
69
PDB code
5vdc
Structure name
crystal structure of the human dpf2 tandem phd finger domain
Structure deposition date
2017-04-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
nan
Peptide accession
Q92785
Residue number A
348
Residue number B
371
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 348 of Zinc finger protein ubi-d4
Cysteine 371 of Zinc finger protein ubi-d4
5b79 A 70 A 74
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 329 and 333 (70 and 74 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
5b79
Structure name
crystal structure of dpf2 double phd finger
Structure deposition date
2016-06-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
49
Minimum pKa ?
5
% buried
2
Peptide accession
Q92785
Residue number A
329
Residue number B
333
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 329 of Zinc finger protein ubi-d4
Cysteine 333 of Zinc finger protein ubi-d4
5vdc A 76 A 102
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 345 and 371 (76 and 102 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
5vdc
Structure name
crystal structure of the human dpf2 tandem phd finger domain
Structure deposition date
2017-04-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
17
% buried
nan
Peptide accession
Q92785
Residue number A
345
Residue number B
371
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 345 of Zinc finger protein ubi-d4
Cysteine 371 of Zinc finger protein ubi-d4
5vdc A 60 A 61
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 329 and 330 (60 and 61 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
5vdc
Structure name
crystal structure of the human dpf2 tandem phd finger domain
Structure deposition date
2017-04-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
7
% buried
18
Peptide accession
Q92785
Residue number A
329
Residue number B
330
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 329 of Zinc finger protein ubi-d4
Cysteine 330 of Zinc finger protein ubi-d4
5vdc A 58 A 60
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 327 and 329 (58 and 60 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
5vdc
Structure name
crystal structure of the human dpf2 tandem phd finger domain
Structure deposition date
2017-04-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
4
Peptide accession
Q92785
Residue number A
327
Residue number B
329
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 327 of Zinc finger protein ubi-d4
Cysteine 329 of Zinc finger protein ubi-d4
5vdc A 26 A 60
A redox-regulated disulphide may form within Zinc finger protein ubi-d4 between cysteines 295 and 329 (26 and 60 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
5vdc
Structure name
crystal structure of the human dpf2 tandem phd finger domain
Structure deposition date
2017-04-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
5
% buried
14
Peptide accession
Q92785
Residue number A
295
Residue number B
329
Peptide name
Zinc finger protein ubi-d4
Ligandability
Cysteine 295 of Zinc finger protein ubi-d4
Cysteine 329 of Zinc finger protein ubi-d4
If this tool was useful for finding a disulphide, please cite: