Disintegrin and metalloproteinase domain-containing protein 33
Intramolecular
Cysteine 361 and cysteine 371
Cysteine 360 and cysteine 388
Cysteine 320 and cysteine 404
Cysteine 360 and cysteine 361
Cysteine 361 and cysteine 388
Cysteine 360 and cysteine 371
Cysteine 371 and cysteine 388
1r54 A 361 A 371
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 33 between cysteines 361 and 371.
Details
Redox score ?
84
PDB code
1r54
Structure name
crystal structure of the catalytic domain of human adam33
Structure deposition date
2003-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ11
Residue number A
361
Residue number B
371
Peptide name
Disintegrin and metalloproteinase domain-containing protein 33
Ligandability
Cysteine 361 of Disintegrin and metalloproteinase domain-containing protein 33
Cysteine 371 of Disintegrin and metalloproteinase domain-containing protein 33
1r54 A 360 A 388
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 33 between cysteines 360 and 388.
Details
Redox score ?
84
PDB code
1r54
Structure name
crystal structure of the catalytic domain of human adam33
Structure deposition date
2003-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ11
Residue number A
360
Residue number B
388
Peptide name
Disintegrin and metalloproteinase domain-containing protein 33
Ligandability
Cysteine 360 of Disintegrin and metalloproteinase domain-containing protein 33
Cysteine 388 of Disintegrin and metalloproteinase domain-containing protein 33
1r55 A 320 A 404
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 33 between cysteines 320 and 404.
Details
Redox score ?
81
PDB code
1r55
Structure name
crystal structure of the catalytic domain of human adam 33
Structure deposition date
2003-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ11
Residue number A
320
Residue number B
404
Peptide name
Disintegrin and metalloproteinase domain-containing protein 33
Ligandability
Cysteine 320 of Disintegrin and metalloproteinase domain-containing protein 33
Cysteine 404 of Disintegrin and metalloproteinase domain-containing protein 33
1r54 A 360 A 361
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 33 between cysteines 360 and 361. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
1r54
Structure name
crystal structure of the catalytic domain of human adam33
Structure deposition date
2003-10-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ11
Residue number A
360
Residue number B
361
Peptide name
Disintegrin and metalloproteinase domain-containing protein 33
Ligandability
Cysteine 360 of Disintegrin and metalloproteinase domain-containing protein 33
Cysteine 361 of Disintegrin and metalloproteinase domain-containing protein 33
1r54 A 361 A 388
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 33 between cysteines 361 and 388. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
1r54
Structure name
crystal structure of the catalytic domain of human adam33
Structure deposition date
2003-10-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ11
Residue number A
361
Residue number B
388
Peptide name
Disintegrin and metalloproteinase domain-containing protein 33
Ligandability
Cysteine 361 of Disintegrin and metalloproteinase domain-containing protein 33
Cysteine 388 of Disintegrin and metalloproteinase domain-containing protein 33
1r55 A 360 A 371
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 33 between cysteines 360 and 371. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
1r55
Structure name
crystal structure of the catalytic domain of human adam 33
Structure deposition date
2003-10-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ11
Residue number A
360
Residue number B
371
Peptide name
Disintegrin and metalloproteinase domain-containing protein 33
Ligandability
Cysteine 360 of Disintegrin and metalloproteinase domain-containing protein 33
Cysteine 371 of Disintegrin and metalloproteinase domain-containing protein 33
1r55 A 371 A 388
A redox-regulated disulphide may form within Disintegrin and metalloproteinase domain-containing protein 33 between cysteines 371 and 388. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
1r55
Structure name
crystal structure of the catalytic domain of human adam 33
Structure deposition date
2003-10-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BZ11
Residue number A
371
Residue number B
388
Peptide name
Disintegrin and metalloproteinase domain-containing protein 33
Ligandability
Cysteine 371 of Disintegrin and metalloproteinase domain-containing protein 33
Cysteine 388 of Disintegrin and metalloproteinase domain-containing protein 33
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