Sentrin-specific protease 1
6nnq A 535 A 602
A redox-regulated disulphide may form within Sentrin-specific protease 1 between cysteines 535 and 603 (535 and 602 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
6nnq
Structure name
non-covalent structure of senp1 in complex with sumo2
Structure deposition date
2019-01-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
89
Minimum pKa ?
11
% buried
84
Peptide accession
Q9P0U3
Residue number A
535
Residue number B
603
Peptide name
Sentrin-specific protease 1
Ligandability
Cysteine 535 of Sentrin-specific protease 1
Cysteine 603 of Sentrin-specific protease 1
2ckg B 602 B 607
A redox-regulated disulphide may form within Sentrin-specific protease 1 between cysteines 603 and 608 (602 and 607 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
2ckg
Structure name
the structure of senp1 sumo-2 co-complex suggests a structural basis for discrimination between sumo paralogues during processing
Structure deposition date
2006-04-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
9
% buried
98
Peptide accession
Q9P0U3
Residue number A
603
Residue number B
608
Peptide name
Sentrin-specific protease 1
Ligandability
Cysteine 603 of Sentrin-specific protease 1
Cysteine 608 of Sentrin-specific protease 1
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