Disintegrin and metalloproteinase domain-containing protein 22
Intramolecular
Cysteine 447 and cysteine 477
Cysteine 460 and cysteine 466
Cysteine 688 and cysteine 700
Cysteine 490 and cysteine 516
Cysteine 702 and cysteine 711
Cysteine 473 and cysteine 494
Cysteine 394 and cysteine 401
Cysteine 503 and cysteine 523
Cysteine 392 and cysteine 417
Cysteine 679 and cysteine 694
More...Cysteine 510 and cysteine 542
Cysteine 458 and cysteine 474
Cysteine 583 and cysteine 593
Cysteine 535 and cysteine 547
Cysteine 569 and cysteine 635
Cysteine 485 and cysteine 491
Cysteine 554 and cysteine 605
Cysteine 657 and cysteine 668
Cysteine 600 and cysteine 663
Cysteine 349 and cysteine 433
Cysteine 510 and cysteine 535
Cysteine 535 and cysteine 542
Cysteine 503 and cysteine 516
Cysteine 490 and cysteine 503
Cysteine 679 and cysteine 700
Cysteine 679 and cysteine 688
Cysteine 700 and cysteine 711
Cysteine 657 and cysteine 663
Cysteine 688 and cysteine 711
Cysteine 600 and cysteine 657
Cysteine 460 and cysteine 474
Cysteine 474 and cysteine 477
Cysteine 490 and cysteine 523
Cysteine 688 and cysteine 694
Cysteine 510 and cysteine 547
Cysteine 473 and cysteine 491
Cysteine 466 and cysteine 474
Cysteine 516 and cysteine 523
Cysteine 700 and cysteine 702
Cysteine 458 and cysteine 477
3g5c B 447 B 477
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 447 and 477.
Details
Redox score ?
87
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
447
Residue number B
477
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 447 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 477 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 460 B 466
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 460 and 466.
Details
Redox score ?
87
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
460
Residue number B
466
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 460 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 466 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 688 A 700
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 688 and 700.
Details
Redox score ?
87
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
688
Residue number B
700
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 688 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 700 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 490 A 516
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 490 and 516.
Details
Redox score ?
86
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
490
Residue number B
516
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 490 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 516 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 702 A 711
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 702 and 711.
Details
Redox score ?
86
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
702
Residue number B
711
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 702 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 711 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 473 B 494
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 473 and 494.
Details
Redox score ?
85
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
473
Residue number B
494
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 473 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 494 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 394 B 401
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 394 and 401.
Details
Redox score ?
85
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
394
Residue number B
401
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 394 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 401 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 503 A 523
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 503 and 523.
Details
Redox score ?
84
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
503
Residue number B
523
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 503 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 523 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 392 B 417
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 392 and 417.
Details
Redox score ?
84
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
392
Residue number B
417
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 392 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 417 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 679 B 694
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 679 and 694.
Details
Redox score ?
84
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
679
Residue number B
694
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 679 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 694 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 510 A 542
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 510 and 542.
Details
Redox score ?
83
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
510
Residue number B
542
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 510 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 542 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 458 A 474
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 458 and 474.
Details
Redox score ?
83
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
458
Residue number B
474
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 458 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 474 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 583 A 593
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 583 and 593.
Details
Redox score ?
83
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
583
Residue number B
593
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 583 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 593 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 535 A 547
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 535 and 547.
Details
Redox score ?
83
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
535
Residue number B
547
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 535 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 547 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 569 B 635
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 569 and 635.
Details
Redox score ?
82
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
569
Residue number B
635
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 569 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 635 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 485 A 491
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 485 and 491.
Details
Redox score ?
82
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
485
Residue number B
491
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 485 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 491 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 554 B 605
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 554 and 605.
Details
Redox score ?
81
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
554
Residue number B
605
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 554 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 605 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 657 A 668
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 657 and 668.
Details
Redox score ?
81
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
657
Residue number B
668
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 657 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 668 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 600 B 663
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 600 and 663.
Details
Redox score ?
81
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
600
Residue number B
663
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 600 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 663 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 349 B 433
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 349 and 433.
Details
Redox score ?
80
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
349
Residue number B
433
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 349 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 433 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 510 B 535
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 510 and 535.
Details
Redox score ?
75
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
510
Residue number B
535
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 510 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 535 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 535 A 542
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 535 and 542.
Details
Redox score ?
75
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
535
Residue number B
542
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 535 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 542 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 503 B 516
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 503 and 516.
Details
Redox score ?
74
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
503
Residue number B
516
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 503 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 516 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 490 B 503
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 490 and 503.
Details
Redox score ?
74
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
490
Residue number B
503
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 490 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 503 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 679 A 700
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 679 and 700.
Details
Redox score ?
74
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
679
Residue number B
700
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 679 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 700 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 679 A 688
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 679 and 688.
Details
Redox score ?
73
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
679
Residue number B
688
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 679 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 688 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 700 A 711
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 700 and 711.
Details
Redox score ?
71
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
700
Residue number B
711
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 700 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 711 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 657 B 663
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 657 and 663.
Details
Redox score ?
70
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
657
Residue number B
663
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 657 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 663 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 688 B 711
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 688 and 711.
Details
Redox score ?
69
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
688
Residue number B
711
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 688 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 711 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 600 B 657
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 600 and 657.
Details
Redox score ?
69
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
600
Residue number B
657
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 600 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 657 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 460 A 474
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 460 and 474.
Details
Redox score ?
68
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
460
Residue number B
474
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 460 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 474 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 474 B 477
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 474 and 477.
Details
Redox score ?
68
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
474
Residue number B
477
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 474 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 477 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 490 B 523
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 490 and 523.
Details
Redox score ?
68
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
490
Residue number B
523
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 490 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 523 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 688 B 694
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 688 and 694.
Details
Redox score ?
65
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
688
Residue number B
694
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 688 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 694 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 510 B 547
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 510 and 547.
Details
Redox score ?
65
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
510
Residue number B
547
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 510 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 547 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 473 A 491
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 473 and 491.
Details
Redox score ?
65
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
473
Residue number B
491
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 473 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 491 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 466 A 474
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 466 and 474.
Details
Redox score ?
64
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
466
Residue number B
474
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 466 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 474 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c B 516 B 523
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 516 and 523.
Details
Redox score ?
64
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
516
Residue number B
523
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 516 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 523 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 700 A 702
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 700 and 702.
Details
Redox score ?
64
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
700
Residue number B
702
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 700 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 702 of Disintegrin and metalloproteinase domain-containing protein 22
3g5c A 458 A 477
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 22 between cysteines 458 and 477.
Details
Redox score ?
63
PDB code
3g5c
Structure name
structural and biochemical studies on the ectodomain of human adam22
Structure deposition date
2009-02-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P0K1
Residue number A
458
Residue number B
477
Peptide name
Disintegrin and metalloproteinase domain-containing protein 22
Ligandability
Cysteine 458 of Disintegrin and metalloproteinase domain-containing protein 22
Cysteine 477 of Disintegrin and metalloproteinase domain-containing protein 22
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