Sentrin-specific protease 2
5aek G 490 G 505
A redox-regulated disulphide may form within Sentrin-specific protease 2 between cysteines 490 and 505. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
5aek
Structure name
crystal structure of the human senp2 c548s in complex with the human sumo1 k48m f66w
Structure deposition date
2014-12-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
48
Peptide accession
Q9HC62
Residue number A
490
Residue number B
505
Peptide name
Sentrin-specific protease 2
Ligandability
Cysteine 490 of Sentrin-specific protease 2
Cysteine 505 of Sentrin-specific protease 2
1tgz A 548 A 553
A redox-regulated disulphide may form within Sentrin-specific protease 2 between cysteines 548 and 553. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
24
PDB code
1tgz
Structure name
structure of human senp2 in complex with sumo-1
Structure deposition date
2004-05-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
92
Peptide accession
Q9HC62
Residue number A
548
Residue number B
553
Peptide name
Sentrin-specific protease 2
Ligandability
Cysteine 548 of Sentrin-specific protease 2
Cysteine 553 of Sentrin-specific protease 2
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