A disintegrin and metalloproteinase with thrombospondin motifs 13
Intramolecular
Cysteine 1236 and cysteine 1254
Cysteine 411 and cysteine 423
Cysteine 322 and cysteine 347
Cysteine 400 and cysteine 438
Cysteine 532 and cysteine 548
Cysteine 545 and cysteine 555
Cysteine 360 and cysteine 371
Cysteine 332 and cysteine 366
Cysteine 396 and cysteine 433
Cysteine 311 and cysteine 337
More...Cysteine 202 and cysteine 281
Cysteine 242 and cysteine 265
Cysteine 1192 and cysteine 1213
Cysteine 1299 and cysteine 1325
Cysteine 450 and cysteine 487
Cysteine 508 and cysteine 527
Cysteine 483 and cysteine 522
Cysteine 332 and cysteine 360
Cysteine 360 and cysteine 366
Cysteine 332 and cysteine 371
Cysteine 483 and cysteine 508
Cysteine 508 and cysteine 522
Cysteine 483 and cysteine 527
Cysteine 522 and cysteine 527
Cysteine 366 and cysteine 371
Cysteine 322 and cysteine 337
Cysteine 311 and cysteine 322
Cysteine 337 and cysteine 347
Cysteine 311 and cysteine 347
Cysteine 396 and cysteine 400
Cysteine 396 and cysteine 438
7b01 A 1236 A 1254
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 1236 and 1254.
Details
Redox score ?
88
PDB code
7b01
Structure name
adamts13-cub12
Structure deposition date
2020-11-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
1236
Residue number B
1254
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 1236 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 1254 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3ghn A 411 A 423
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 411 and 423.
Details
Redox score ?
87
PDB code
3ghn
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (form-2)
Structure deposition date
2009-03-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
411
Residue number B
423
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 411 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 423 of A disintegrin and metalloproteinase with thrombospondin motifs 13
6qig A 322 A 347
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 322 and 347.
Details
Redox score ?
87
PDB code
6qig
Structure name
metalloproteinase
Structure deposition date
2019-01-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
322
Residue number B
347
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 322 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 347 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3ghm A 400 A 438
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 400 and 438.
Details
Redox score ?
86
PDB code
3ghm
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (form-1)
Structure deposition date
2009-03-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
40
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
400
Residue number B
438
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 400 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 438 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3vn4 A 532 A 548
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 532 and 548.
Details
Redox score ?
86
PDB code
3vn4
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (p475s mutant)
Structure deposition date
2011-12-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
532
Residue number B
548
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 532 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 548 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3ghn A 545 A 555
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 545 and 555.
Details
Redox score ?
85
PDB code
3ghn
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (form-2)
Structure deposition date
2009-03-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
545
Residue number B
555
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 545 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 555 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3ghn A 360 A 371
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 360 and 371.
Details
Redox score ?
85
PDB code
3ghn
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (form-2)
Structure deposition date
2009-03-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
360
Residue number B
371
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 360 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 371 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3ghn A 332 A 366
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 332 and 366.
Details
Redox score ?
84
PDB code
3ghn
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (form-2)
Structure deposition date
2009-03-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
332
Residue number B
366
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 332 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 366 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3vn4 A 396 A 433
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 396 and 433.
Details
Redox score ?
84
PDB code
3vn4
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (p475s mutant)
Structure deposition date
2011-12-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
396
Residue number B
433
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 396 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 433 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3ghm A 311 A 337
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 311 and 337.
Details
Redox score ?
84
PDB code
3ghm
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (form-1)
Structure deposition date
2009-03-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
311
Residue number B
337
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 311 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 337 of A disintegrin and metalloproteinase with thrombospondin motifs 13
6qig A 202 A 281
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 202 and 281.
Details
Redox score ?
83
PDB code
6qig
Structure name
metalloproteinase
Structure deposition date
2019-01-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
202
Residue number B
281
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 202 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 281 of A disintegrin and metalloproteinase with thrombospondin motifs 13
6qig A 242 A 265
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 242 and 265.
Details
Redox score ?
83
PDB code
6qig
Structure name
metalloproteinase
Structure deposition date
2019-01-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
242
Residue number B
265
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 242 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 265 of A disintegrin and metalloproteinase with thrombospondin motifs 13
7b01 A 1192 A 1213
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 1192 and 1213.
Details
Redox score ?
83
PDB code
7b01
Structure name
adamts13-cub12
Structure deposition date
2020-11-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
1192
Residue number B
1213
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 1192 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 1213 of A disintegrin and metalloproteinase with thrombospondin motifs 13
7b01 A 1299 A 1325
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 1299 and 1325.
Details
Redox score ?
83
PDB code
7b01
Structure name
adamts13-cub12
Structure deposition date
2020-11-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
1299
Residue number B
1325
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 1299 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 1325 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3ghn A 450 A 487
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 450 and 487.
Details
Redox score ?
82
PDB code
3ghn
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (form-2)
Structure deposition date
2009-03-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
450
Residue number B
487
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 450 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 487 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3vn4 A 508 A 527
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 508 and 527.
Details
Redox score ?
82
PDB code
3vn4
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (p475s mutant)
Structure deposition date
2011-12-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
508
Residue number B
527
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 508 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 527 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3ghn A 483 A 522
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 483 and 522.
Details
Redox score ?
80
PDB code
3ghn
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (form-2)
Structure deposition date
2009-03-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
483
Residue number B
522
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 483 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 522 of A disintegrin and metalloproteinase with thrombospondin motifs 13
6qig A 332 A 360
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 332 and 360.
Details
Redox score ?
77
PDB code
6qig
Structure name
metalloproteinase
Structure deposition date
2019-01-18
Thiol separation (Å)
3
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
332
Residue number B
360
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 332 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 360 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3ghm A 360 A 366
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 360 and 366.
Details
Redox score ?
72
PDB code
3ghm
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (form-1)
Structure deposition date
2009-03-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
360
Residue number B
366
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 360 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 366 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3ghn A 332 A 371
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 332 and 371.
Details
Redox score ?
72
PDB code
3ghn
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (form-2)
Structure deposition date
2009-03-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
332
Residue number B
371
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 332 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 371 of A disintegrin and metalloproteinase with thrombospondin motifs 13
6qig A 483 A 508
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 483 and 508.
Details
Redox score ?
71
PDB code
6qig
Structure name
metalloproteinase
Structure deposition date
2019-01-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
483
Residue number B
508
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 483 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 508 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3vn4 A 508 A 522
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 508 and 522.
Details
Redox score ?
67
PDB code
3vn4
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (p475s mutant)
Structure deposition date
2011-12-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
508
Residue number B
522
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 508 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 522 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3ghn A 483 A 527
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 483 and 527.
Details
Redox score ?
67
PDB code
3ghn
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (form-2)
Structure deposition date
2009-03-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
483
Residue number B
527
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 483 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 527 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3ghn A 522 A 527
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 522 and 527.
Details
Redox score ?
61
PDB code
3ghn
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (form-2)
Structure deposition date
2009-03-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
522
Residue number B
527
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 522 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 527 of A disintegrin and metalloproteinase with thrombospondin motifs 13
6qig A 366 A 371
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 366 and 371. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
60
PDB code
6qig
Structure name
metalloproteinase
Structure deposition date
2019-01-18
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
366
Residue number B
371
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 366 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 371 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3vn4 A 322 A 337
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 322 and 337. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
3vn4
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (p475s mutant)
Structure deposition date
2011-12-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
322
Residue number B
337
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 322 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 337 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3vn4 A 311 A 322
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 311 and 322. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
3vn4
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (p475s mutant)
Structure deposition date
2011-12-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
311
Residue number B
322
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 311 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 322 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3ghm A 337 A 347
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 337 and 347. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
3ghm
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (form-1)
Structure deposition date
2009-03-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
337
Residue number B
347
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 337 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 347 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3ghn A 311 A 347
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 311 and 347. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
3ghn
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (form-2)
Structure deposition date
2009-03-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
311
Residue number B
347
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 311 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 347 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3ghn A 396 A 400
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 396 and 400. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
3ghn
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (form-2)
Structure deposition date
2009-03-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
396
Residue number B
400
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 396 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 400 of A disintegrin and metalloproteinase with thrombospondin motifs 13
3ghn A 396 A 438
A redox-regulated disulphide may form within A disintegrin and metalloproteinase with thrombospondin motifs 13 between cysteines 396 and 438. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
3ghn
Structure name
crystal structure of the exosite-containing fragment of human adamts13 (form-2)
Structure deposition date
2009-03-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q76LX8
Residue number A
396
Residue number B
438
Peptide name
A disintegrin and metalloproteinase with thrombospondin motifs 13
Ligandability
Cysteine 396 of A disintegrin and metalloproteinase with thrombospondin motifs 13
Cysteine 438 of A disintegrin and metalloproteinase with thrombospondin motifs 13
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