Delta-like protein 4
Intramolecular
Cysteine 226 and cysteine 239
Cysteine 312 and cysteine 321
Cysteine 50 and cysteine 54
Cysteine 294 and cysteine 310
Cysteine 259 and cysteine 270
Cysteine 288 and cysteine 300
Cysteine 222 and cysteine 233
Cysteine 208 and cysteine 217
Cysteine 188 and cysteine 200
Cysteine 272 and cysteine 281
More...Cysteine 175 and cysteine 184
Cysteine 241 and cysteine 250
Cysteine 253 and cysteine 264
Cysteine 61 and cysteine 74
Cysteine 270 and cysteine 281
Cysteine 239 and cysteine 250
Cysteine 294 and cysteine 300
Cysteine 259 and cysteine 281
Cysteine 222 and cysteine 226
Cysteine 310 and cysteine 321
Cysteine 226 and cysteine 250
Cysteine 300 and cysteine 310
Cysteine 270 and cysteine 272
Cysteine 239 and cysteine 241
Cysteine 294 and cysteine 321
Cysteine 288 and cysteine 294
Cysteine 226 and cysteine 233
Cysteine 222 and cysteine 239
Cysteine 259 and cysteine 272
Cysteine 310 and cysteine 312
Cysteine 288 and cysteine 310
Cysteine 226 and cysteine 241
Cysteine 233 and cysteine 239
Cysteine 259 and cysteine 264
Cysteine 294 and cysteine 312
Cysteine 264 and cysteine 270
Cysteine 188 and cysteine 217
Cysteine 222 and cysteine 250
Cysteine 300 and cysteine 321
Cysteine 200 and cysteine 217
5mvx A 226 A 239
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 226 and 239.
Details
Redox score ?
89
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
226
Residue number B
239
Peptide name
Delta-like protein 4
Ligandability
Cysteine 226 of Delta-like protein 4
Cysteine 239 of Delta-like protein 4
5mvx A 312 A 321
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 312 and 321.
Details
Redox score ?
88
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
312
Residue number B
321
Peptide name
Delta-like protein 4
Ligandability
Cysteine 312 of Delta-like protein 4
Cysteine 321 of Delta-like protein 4
5mvx A 50 A 54
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 50 and 54.
Details
Redox score ?
88
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
50
Residue number B
54
Peptide name
Delta-like protein 4
Ligandability
Cysteine 50 of Delta-like protein 4
Cysteine 54 of Delta-like protein 4
5mvx A 294 A 310
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 294 and 310.
Details
Redox score ?
88
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
294
Residue number B
310
Peptide name
Delta-like protein 4
Ligandability
Cysteine 294 of Delta-like protein 4
Cysteine 310 of Delta-like protein 4
5mvx A 259 A 270
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 259 and 270.
Details
Redox score ?
88
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
259
Residue number B
270
Peptide name
Delta-like protein 4
Ligandability
Cysteine 259 of Delta-like protein 4
Cysteine 270 of Delta-like protein 4
5mvx A 288 A 300
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 288 and 300.
Details
Redox score ?
88
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
288
Residue number B
300
Peptide name
Delta-like protein 4
Ligandability
Cysteine 288 of Delta-like protein 4
Cysteine 300 of Delta-like protein 4
5mvx A 222 A 233
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 222 and 233.
Details
Redox score ?
87
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
222
Residue number B
233
Peptide name
Delta-like protein 4
Ligandability
Cysteine 222 of Delta-like protein 4
Cysteine 233 of Delta-like protein 4
5mvx A 208 A 217
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 208 and 217.
Details
Redox score ?
87
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
208
Residue number B
217
Peptide name
Delta-like protein 4
Ligandability
Cysteine 208 of Delta-like protein 4
Cysteine 217 of Delta-like protein 4
5mvx A 188 A 200
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 188 and 200.
Details
Redox score ?
87
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
188
Residue number B
200
Peptide name
Delta-like protein 4
Ligandability
Cysteine 188 of Delta-like protein 4
Cysteine 200 of Delta-like protein 4
5mvx A 272 A 281
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 272 and 281.
Details
Redox score ?
86
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
272
Residue number B
281
Peptide name
Delta-like protein 4
Ligandability
Cysteine 272 of Delta-like protein 4
Cysteine 281 of Delta-like protein 4
5mvx A 175 A 184
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 175 and 184.
Details
Redox score ?
86
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
175
Residue number B
184
Peptide name
Delta-like protein 4
Ligandability
Cysteine 175 of Delta-like protein 4
Cysteine 184 of Delta-like protein 4
5mvx A 241 A 250
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 241 and 250.
Details
Redox score ?
86
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
241
Residue number B
250
Peptide name
Delta-like protein 4
Ligandability
Cysteine 241 of Delta-like protein 4
Cysteine 250 of Delta-like protein 4
5mvx A 253 A 264
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 253 and 264.
Details
Redox score ?
85
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
253
Residue number B
264
Peptide name
Delta-like protein 4
Ligandability
Cysteine 253 of Delta-like protein 4
Cysteine 264 of Delta-like protein 4
5mvx A 61 A 74
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 61 and 74.
Details
Redox score ?
82
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
61
Residue number B
74
Peptide name
Delta-like protein 4
Ligandability
Cysteine 61 of Delta-like protein 4
Cysteine 74 of Delta-like protein 4
5mvx A 270 A 281
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 270 and 281.
Details
Redox score ?
78
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
270
Residue number B
281
Peptide name
Delta-like protein 4
Ligandability
Cysteine 270 of Delta-like protein 4
Cysteine 281 of Delta-like protein 4
5mvx A 239 A 250
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 239 and 250.
Details
Redox score ?
78
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
239
Residue number B
250
Peptide name
Delta-like protein 4
Ligandability
Cysteine 239 of Delta-like protein 4
Cysteine 250 of Delta-like protein 4
5mvx A 294 A 300
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 294 and 300.
Details
Redox score ?
77
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
294
Residue number B
300
Peptide name
Delta-like protein 4
Ligandability
Cysteine 294 of Delta-like protein 4
Cysteine 300 of Delta-like protein 4
5mvx A 259 A 281
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 259 and 281.
Details
Redox score ?
73
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
259
Residue number B
281
Peptide name
Delta-like protein 4
Ligandability
Cysteine 259 of Delta-like protein 4
Cysteine 281 of Delta-like protein 4
5mvx A 222 A 226
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 222 and 226.
Details
Redox score ?
73
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
222
Residue number B
226
Peptide name
Delta-like protein 4
Ligandability
Cysteine 222 of Delta-like protein 4
Cysteine 226 of Delta-like protein 4
5mvx A 310 A 321
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 310 and 321.
Details
Redox score ?
71
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
310
Residue number B
321
Peptide name
Delta-like protein 4
Ligandability
Cysteine 310 of Delta-like protein 4
Cysteine 321 of Delta-like protein 4
5mvx A 226 A 250
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 226 and 250.
Details
Redox score ?
69
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
226
Residue number B
250
Peptide name
Delta-like protein 4
Ligandability
Cysteine 226 of Delta-like protein 4
Cysteine 250 of Delta-like protein 4
5mvx A 300 A 310
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 300 and 310.
Details
Redox score ?
69
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
300
Residue number B
310
Peptide name
Delta-like protein 4
Ligandability
Cysteine 300 of Delta-like protein 4
Cysteine 310 of Delta-like protein 4
5mvx A 270 A 272
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 270 and 272.
Details
Redox score ?
67
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
270
Residue number B
272
Peptide name
Delta-like protein 4
Ligandability
Cysteine 270 of Delta-like protein 4
Cysteine 272 of Delta-like protein 4
5mvx A 239 A 241
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 239 and 241.
Details
Redox score ?
67
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
239
Residue number B
241
Peptide name
Delta-like protein 4
Ligandability
Cysteine 239 of Delta-like protein 4
Cysteine 241 of Delta-like protein 4
5mvx A 294 A 321
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 294 and 321.
Details
Redox score ?
66
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
294
Residue number B
321
Peptide name
Delta-like protein 4
Ligandability
Cysteine 294 of Delta-like protein 4
Cysteine 321 of Delta-like protein 4
5mvx A 288 A 294
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 288 and 294.
Details
Redox score ?
66
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
288
Residue number B
294
Peptide name
Delta-like protein 4
Ligandability
Cysteine 288 of Delta-like protein 4
Cysteine 294 of Delta-like protein 4
5mvx A 226 A 233
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 226 and 233.
Details
Redox score ?
65
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
226
Residue number B
233
Peptide name
Delta-like protein 4
Ligandability
Cysteine 226 of Delta-like protein 4
Cysteine 233 of Delta-like protein 4
5mvx A 222 A 239
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 222 and 239.
Details
Redox score ?
62
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
222
Residue number B
239
Peptide name
Delta-like protein 4
Ligandability
Cysteine 222 of Delta-like protein 4
Cysteine 239 of Delta-like protein 4
5mvx A 259 A 272
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 259 and 272.
Details
Redox score ?
61
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
259
Residue number B
272
Peptide name
Delta-like protein 4
Ligandability
Cysteine 259 of Delta-like protein 4
Cysteine 272 of Delta-like protein 4
5mvx A 310 A 312
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 310 and 312.
Details
Redox score ?
60
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
310
Residue number B
312
Peptide name
Delta-like protein 4
Ligandability
Cysteine 310 of Delta-like protein 4
Cysteine 312 of Delta-like protein 4
5mvx A 288 A 310
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 288 and 310. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
288
Residue number B
310
Peptide name
Delta-like protein 4
Ligandability
Cysteine 288 of Delta-like protein 4
Cysteine 310 of Delta-like protein 4
5mvx A 226 A 241
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 226 and 241. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
226
Residue number B
241
Peptide name
Delta-like protein 4
Ligandability
Cysteine 226 of Delta-like protein 4
Cysteine 241 of Delta-like protein 4
5mvx A 233 A 239
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 233 and 239. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
233
Residue number B
239
Peptide name
Delta-like protein 4
Ligandability
Cysteine 233 of Delta-like protein 4
Cysteine 239 of Delta-like protein 4
5mvx A 259 A 264
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 259 and 264. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
259
Residue number B
264
Peptide name
Delta-like protein 4
Ligandability
Cysteine 259 of Delta-like protein 4
Cysteine 264 of Delta-like protein 4
5mvx A 294 A 312
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 294 and 312. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
294
Residue number B
312
Peptide name
Delta-like protein 4
Ligandability
Cysteine 294 of Delta-like protein 4
Cysteine 312 of Delta-like protein 4
5mvx A 264 A 270
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 264 and 270. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
264
Residue number B
270
Peptide name
Delta-like protein 4
Ligandability
Cysteine 264 of Delta-like protein 4
Cysteine 270 of Delta-like protein 4
5mvx A 188 A 217
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 188 and 217. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
188
Residue number B
217
Peptide name
Delta-like protein 4
Ligandability
Cysteine 188 of Delta-like protein 4
Cysteine 217 of Delta-like protein 4
5mvx A 222 A 250
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 222 and 250. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
222
Residue number B
250
Peptide name
Delta-like protein 4
Ligandability
Cysteine 222 of Delta-like protein 4
Cysteine 250 of Delta-like protein 4
5mvx A 300 A 321
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 300 and 321. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
300
Residue number B
321
Peptide name
Delta-like protein 4
Ligandability
Cysteine 300 of Delta-like protein 4
Cysteine 321 of Delta-like protein 4
5mvx A 200 A 217
A redox-regulated disulphide may form within Delta-like protein 4 between cysteines 200 and 217. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
5mvx
Structure name
human dll4 c2-egf3
Structure deposition date
2017-01-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NR61
Residue number A
200
Residue number B
217
Peptide name
Delta-like protein 4
Ligandability
Cysteine 200 of Delta-like protein 4
Cysteine 217 of Delta-like protein 4
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