E3 ubiquitin-protein ligase parkin
Intermolecular
Cysteine 352 and cysteine 323
Intramolecular
Cysteine 421 and cysteine 441
Cysteine 253 and cysteine 293
Cysteine 253 and cysteine 289
Cysteine 365 and cysteine 377
Cysteine 150 and cysteine 154
Cysteine 169 and cysteine 196
Cysteine 365 and cysteine 368
Cysteine 421 and cysteine 436
Cysteine 352 and cysteine 360
More...Cysteine 418 and cysteine 436
Cysteine 337 and cysteine 352
Cysteine 436 and cysteine 441
Cysteine 418 and cysteine 421
Cysteine 166 and cysteine 201
Cysteine 337 and cysteine 360
Cysteine 446 and cysteine 457
Cysteine 196 and cysteine 201
Cysteine 166 and cysteine 169
Cysteine 368 and cysteine 377
Cysteine 332 and cysteine 352
Cysteine 154 and cysteine 212
Cysteine 166 and cysteine 196
Cysteine 332 and cysteine 360
Cysteine 446 and cysteine 449
Cysteine 332 and cysteine 337
Cysteine 418 and cysteine 441
Cysteine 260 and cysteine 263
Cysteine 169 and cysteine 201
Cysteine 289 and cysteine 293
Cysteine 451 and cysteine 457
Cysteine 241 and cysteine 260
Cysteine 446 and cysteine 451
Cysteine 150 and cysteine 212
Cysteine 449 and cysteine 451
Cysteine 449 and cysteine 457
Cysteine 238 and cysteine 241
Cysteine 241 and cysteine 263
Cysteine 238 and cysteine 260
Cysteine 238 and cysteine 263
4k7d A 352 B 323
A redox-regulated disulphide may form between two units of E3 ubiquitin-protein ligase parkin at cysteines 352 and 323. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
4k7d
Structure name
crystal structure of parkin c-terminal ring domains
Structure deposition date
2013-04-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
6
% buried
56
Peptide A name
E3 ubiquitin-protein ligase parkin
Peptide B name
E3 ubiquitin-protein ligase parkin
Peptide A accession
Q9JK66
Peptide B accession
Q9JK66
Peptide A residue number
352
Peptide B residue number
323
Ligandability
Cysteine 352 of E3 ubiquitin-protein ligase parkin
Cysteine 323 of E3 ubiquitin-protein ligase parkin
5c23 B 421 B 441
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 421 and 441.
Details
Redox score ?
88
PDB code
5c23
Structure name
parkin (s65dublr0rbr)
Structure deposition date
2015-06-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
6
% buried
0
Peptide accession
O60260
Residue number A
421
Residue number B
441
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 421 of E3 ubiquitin-protein ligase parkin
Cysteine 441 of E3 ubiquitin-protein ligase parkin
6glc A 253 A 293
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 253 and 293.
Details
Redox score ?
88
PDB code
6glc
Structure name
structure of phospho-parkin bound to phospho-ubiquitin
Structure deposition date
2018-05-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
6
% buried
2
Peptide accession
O60260
Residue number A
253
Residue number B
293
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 253 of E3 ubiquitin-protein ligase parkin
Cysteine 293 of E3 ubiquitin-protein ligase parkin
6hue B 253 B 289
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 253 and 289.
Details
Redox score ?
87
PDB code
6hue
Structure name
parkins65n
Structure deposition date
2018-10-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
4
% buried
60
Peptide accession
O60260
Residue number A
253
Residue number B
289
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 253 of E3 ubiquitin-protein ligase parkin
Cysteine 289 of E3 ubiquitin-protein ligase parkin
5c23 A 365 A 377
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 365 and 377.
Details
Redox score ?
87
PDB code
5c23
Structure name
parkin (s65dublr0rbr)
Structure deposition date
2015-06-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
4
Peptide accession
O60260
Residue number A
365
Residue number B
377
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 365 of E3 ubiquitin-protein ligase parkin
Cysteine 377 of E3 ubiquitin-protein ligase parkin
5c9v A 150 A 154
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 150 and 154.
Details
Redox score ?
85
PDB code
5c9v
Structure name
structure of human parkin g319a
Structure deposition date
2015-06-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
8
Peptide accession
O60260
Residue number A
150
Residue number B
154
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 150 of E3 ubiquitin-protein ligase parkin
Cysteine 154 of E3 ubiquitin-protein ligase parkin
5c23 B 169 B 196
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 169 and 196.
Details
Redox score ?
84
PDB code
5c23
Structure name
parkin (s65dublr0rbr)
Structure deposition date
2015-06-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
6
% buried
22
Peptide accession
O60260
Residue number A
169
Residue number B
196
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 169 of E3 ubiquitin-protein ligase parkin
Cysteine 196 of E3 ubiquitin-protein ligase parkin
5n2w A 365 A 368
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 365 and 368.
Details
Redox score ?
84
PDB code
5n2w
Structure name
wt-parkin and pub complex
Structure deposition date
2017-02-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
6
% buried
0
Peptide accession
O60260
Residue number A
365
Residue number B
368
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 365 of E3 ubiquitin-protein ligase parkin
Cysteine 368 of E3 ubiquitin-protein ligase parkin
6hue A 421 A 436
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 421 and 436.
Details
Redox score ?
84
PDB code
6hue
Structure name
parkins65n
Structure deposition date
2018-10-07
Thiol separation (Å)
3
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
0
Peptide accession
O60260
Residue number A
421
Residue number B
436
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 421 of E3 ubiquitin-protein ligase parkin
Cysteine 436 of E3 ubiquitin-protein ligase parkin
4k95 B 352 B 360
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 352 and 360.
Details
Redox score ?
84
PDB code
4k95
Structure name
crystal structure of parkin
Structure deposition date
2013-04-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
6
% buried
16
Peptide accession
Q9JK66
Residue number A
352
Residue number B
360
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 352 of E3 ubiquitin-protein ligase parkin
Cysteine 360 of E3 ubiquitin-protein ligase parkin
5n38 A 418 A 436
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 418 and 436.
Details
Redox score ?
84
PDB code
5n38
Structure name
s65dparkin and pub complex
Structure deposition date
2017-02-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
7
% buried
2
Peptide accession
O60260
Residue number A
418
Residue number B
436
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 418 of E3 ubiquitin-protein ligase parkin
Cysteine 436 of E3 ubiquitin-protein ligase parkin
4k95 G 337 G 352
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 337 and 352.
Details
Redox score ?
83
PDB code
4k95
Structure name
crystal structure of parkin
Structure deposition date
2013-04-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
7
% buried
20
Peptide accession
Q9JK66
Residue number A
337
Residue number B
352
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 337 of E3 ubiquitin-protein ligase parkin
Cysteine 352 of E3 ubiquitin-protein ligase parkin
6hue A 436 A 441
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 436 and 441.
Details
Redox score ?
83
PDB code
6hue
Structure name
parkins65n
Structure deposition date
2018-10-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
7
% buried
0
Peptide accession
O60260
Residue number A
436
Residue number B
441
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 436 of E3 ubiquitin-protein ligase parkin
Cysteine 441 of E3 ubiquitin-protein ligase parkin
5n2w A 418 A 421
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 418 and 421.
Details
Redox score ?
83
PDB code
5n2w
Structure name
wt-parkin and pub complex
Structure deposition date
2017-02-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
0
Peptide accession
O60260
Residue number A
418
Residue number B
421
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 418 of E3 ubiquitin-protein ligase parkin
Cysteine 421 of E3 ubiquitin-protein ligase parkin
5c23 A 166 A 201
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 166 and 201.
Details
Redox score ?
82
PDB code
5c23
Structure name
parkin (s65dublr0rbr)
Structure deposition date
2015-06-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
29
Peptide accession
O60260
Residue number A
166
Residue number B
201
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 166 of E3 ubiquitin-protein ligase parkin
Cysteine 201 of E3 ubiquitin-protein ligase parkin
5n2w A 337 A 360
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 337 and 360.
Details
Redox score ?
82
PDB code
5n2w
Structure name
wt-parkin and pub complex
Structure deposition date
2017-02-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
17
Peptide accession
O60260
Residue number A
337
Residue number B
360
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 337 of E3 ubiquitin-protein ligase parkin
Cysteine 360 of E3 ubiquitin-protein ligase parkin
5c9v A 446 A 457
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 446 and 457.
Details
Redox score ?
82
PDB code
5c9v
Structure name
structure of human parkin g319a
Structure deposition date
2015-06-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
6
% buried
36
Peptide accession
O60260
Residue number A
446
Residue number B
457
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 446 of E3 ubiquitin-protein ligase parkin
Cysteine 457 of E3 ubiquitin-protein ligase parkin
4i1f A 196 A 201
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 196 and 201.
Details
Redox score ?
82
PDB code
4i1f
Structure name
structure of parkin-s223p e3 ligase
Structure deposition date
2012-11-20
Thiol separation (Å)
3
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60260
Residue number A
196
Residue number B
201
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 196 of E3 ubiquitin-protein ligase parkin
Cysteine 201 of E3 ubiquitin-protein ligase parkin
6hue A 166 A 169
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 166 and 169.
Details
Redox score ?
81
PDB code
6hue
Structure name
parkins65n
Structure deposition date
2018-10-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
6
% buried
36
Peptide accession
O60260
Residue number A
166
Residue number B
169
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 166 of E3 ubiquitin-protein ligase parkin
Cysteine 169 of E3 ubiquitin-protein ligase parkin
6hue B 368 B 377
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 368 and 377.
Details
Redox score ?
81
PDB code
6hue
Structure name
parkins65n
Structure deposition date
2018-10-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
8
Peptide accession
O60260
Residue number A
368
Residue number B
377
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 368 of E3 ubiquitin-protein ligase parkin
Cysteine 377 of E3 ubiquitin-protein ligase parkin
4k95 B 332 B 352
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 332 and 352.
Details
Redox score ?
80
PDB code
4k95
Structure name
crystal structure of parkin
Structure deposition date
2013-04-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
7
% buried
26
Peptide accession
Q9JK66
Residue number A
332
Residue number B
352
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 332 of E3 ubiquitin-protein ligase parkin
Cysteine 352 of E3 ubiquitin-protein ligase parkin
6hue A 154 A 212
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 154 and 212.
Details
Redox score ?
80
PDB code
6hue
Structure name
parkins65n
Structure deposition date
2018-10-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
7
% buried
30
Peptide accession
O60260
Residue number A
154
Residue number B
212
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 154 of E3 ubiquitin-protein ligase parkin
Cysteine 212 of E3 ubiquitin-protein ligase parkin
4i1f A 166 A 196
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 166 and 196.
Details
Redox score ?
79
PDB code
4i1f
Structure name
structure of parkin-s223p e3 ligase
Structure deposition date
2012-11-20
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60260
Residue number A
166
Residue number B
196
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 166 of E3 ubiquitin-protein ligase parkin
Cysteine 196 of E3 ubiquitin-protein ligase parkin
4k95 L 332 L 360
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 332 and 360.
Details
Redox score ?
78
PDB code
4k95
Structure name
crystal structure of parkin
Structure deposition date
2013-04-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
7
% buried
38
Peptide accession
Q9JK66
Residue number A
332
Residue number B
360
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 332 of E3 ubiquitin-protein ligase parkin
Cysteine 360 of E3 ubiquitin-protein ligase parkin
6hue B 446 B 449
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 446 and 449.
Details
Redox score ?
78
PDB code
6hue
Structure name
parkins65n
Structure deposition date
2018-10-07
Thiol separation (Å)
3
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
32
Peptide accession
O60260
Residue number A
446
Residue number B
449
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 446 of E3 ubiquitin-protein ligase parkin
Cysteine 449 of E3 ubiquitin-protein ligase parkin
6hue A 332 A 337
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 332 and 337.
Details
Redox score ?
77
PDB code
6hue
Structure name
parkins65n
Structure deposition date
2018-10-07
Thiol separation (Å)
3
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
24
Peptide accession
O60260
Residue number A
332
Residue number B
337
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 332 of E3 ubiquitin-protein ligase parkin
Cysteine 337 of E3 ubiquitin-protein ligase parkin
4i1f A 418 A 441
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 418 and 441.
Details
Redox score ?
77
PDB code
4i1f
Structure name
structure of parkin-s223p e3 ligase
Structure deposition date
2012-11-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60260
Residue number A
418
Residue number B
441
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 418 of E3 ubiquitin-protein ligase parkin
Cysteine 441 of E3 ubiquitin-protein ligase parkin
5c23 B 260 B 263
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 260 and 263.
Details
Redox score ?
76
PDB code
5c23
Structure name
parkin (s65dublr0rbr)
Structure deposition date
2015-06-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
6
% buried
89
Peptide accession
O60260
Residue number A
260
Residue number B
263
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 260 of E3 ubiquitin-protein ligase parkin
Cysteine 263 of E3 ubiquitin-protein ligase parkin
4i1f A 169 A 201
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 169 and 201.
Details
Redox score ?
76
PDB code
4i1f
Structure name
structure of parkin-s223p e3 ligase
Structure deposition date
2012-11-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60260
Residue number A
169
Residue number B
201
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 169 of E3 ubiquitin-protein ligase parkin
Cysteine 201 of E3 ubiquitin-protein ligase parkin
4k7d A 289 A 293
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 289 and 293.
Details
Redox score ?
76
PDB code
4k7d
Structure name
crystal structure of parkin c-terminal ring domains
Structure deposition date
2013-04-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
44
Peptide accession
Q9JK66
Residue number A
289
Residue number B
293
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 289 of E3 ubiquitin-protein ligase parkin
Cysteine 293 of E3 ubiquitin-protein ligase parkin
5c23 B 451 B 457
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 451 and 457.
Details
Redox score ?
76
PDB code
5c23
Structure name
parkin (s65dublr0rbr)
Structure deposition date
2015-06-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
14
Peptide accession
O60260
Residue number A
451
Residue number B
457
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 451 of E3 ubiquitin-protein ligase parkin
Cysteine 457 of E3 ubiquitin-protein ligase parkin
5c23 A 241 A 260
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 241 and 260.
Details
Redox score ?
75
PDB code
5c23
Structure name
parkin (s65dublr0rbr)
Structure deposition date
2015-06-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
6
% buried
78
Peptide accession
O60260
Residue number A
241
Residue number B
260
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 241 of E3 ubiquitin-protein ligase parkin
Cysteine 260 of E3 ubiquitin-protein ligase parkin
5n38 A 446 A 451
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 446 and 451.
Details
Redox score ?
74
PDB code
5n38
Structure name
s65dparkin and pub complex
Structure deposition date
2017-02-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
34
Peptide accession
O60260
Residue number A
446
Residue number B
451
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 446 of E3 ubiquitin-protein ligase parkin
Cysteine 451 of E3 ubiquitin-protein ligase parkin
4i1f A 150 A 212
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 150 and 212.
Details
Redox score ?
74
PDB code
4i1f
Structure name
structure of parkin-s223p e3 ligase
Structure deposition date
2012-11-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60260
Residue number A
150
Residue number B
212
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 150 of E3 ubiquitin-protein ligase parkin
Cysteine 212 of E3 ubiquitin-protein ligase parkin
5n2w A 449 A 451
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 449 and 451.
Details
Redox score ?
74
PDB code
5n2w
Structure name
wt-parkin and pub complex
Structure deposition date
2017-02-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
16
Peptide accession
O60260
Residue number A
449
Residue number B
451
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 449 of E3 ubiquitin-protein ligase parkin
Cysteine 451 of E3 ubiquitin-protein ligase parkin
4i1f A 449 A 457
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 449 and 457.
Details
Redox score ?
73
PDB code
4i1f
Structure name
structure of parkin-s223p e3 ligase
Structure deposition date
2012-11-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60260
Residue number A
449
Residue number B
457
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 449 of E3 ubiquitin-protein ligase parkin
Cysteine 457 of E3 ubiquitin-protein ligase parkin
6hue B 238 B 241
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 238 and 241.
Details
Redox score ?
70
PDB code
6hue
Structure name
parkins65n
Structure deposition date
2018-10-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
nan
Peptide accession
O60260
Residue number A
238
Residue number B
241
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 238 of E3 ubiquitin-protein ligase parkin
Cysteine 241 of E3 ubiquitin-protein ligase parkin
6hue B 241 B 263
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 241 and 263.
Details
Redox score ?
68
PDB code
6hue
Structure name
parkins65n
Structure deposition date
2018-10-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
74
Peptide accession
O60260
Residue number A
241
Residue number B
263
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 241 of E3 ubiquitin-protein ligase parkin
Cysteine 263 of E3 ubiquitin-protein ligase parkin
6hue A 238 A 260
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 238 and 260.
Details
Redox score ?
67
PDB code
6hue
Structure name
parkins65n
Structure deposition date
2018-10-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
10
% buried
nan
Peptide accession
O60260
Residue number A
238
Residue number B
260
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 238 of E3 ubiquitin-protein ligase parkin
Cysteine 260 of E3 ubiquitin-protein ligase parkin
5n38 A 238 A 263
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 238 and 263. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
5n38
Structure name
s65dparkin and pub complex
Structure deposition date
2017-02-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
19
% buried
nan
Peptide accession
O60260
Residue number A
238
Residue number B
263
Peptide name
E3 ubiquitin-protein ligase parkin
Ligandability
Cysteine 238 of E3 ubiquitin-protein ligase parkin
Cysteine 263 of E3 ubiquitin-protein ligase parkin
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