Aspartyl/asparaginyl beta-hydroxylase
5jz6 A 641 A 648
A redox-regulated disulphide may form within Aspartyl/asparaginyl beta-hydroxylase between cysteines 641 and 648.
Details
Redox score ?
84
PDB code
5jz6
Structure name
aspartyl/asparaginyl beta-hydroxylase (asph)oxygenase and tpr domains in complex with manganese and l-malate
Structure deposition date
2016-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q12797
Residue number A
641
Residue number B
648
Peptide name
Aspartyl/asparaginyl beta-hydroxylase
Ligandability
Cysteine 641 of Aspartyl/asparaginyl beta-hydroxylase
Cysteine 648 of Aspartyl/asparaginyl beta-hydroxylase
6q9f A 660 A 685
A redox-regulated disulphide may form within Aspartyl/asparaginyl beta-hydroxylase between cysteines 660 and 685. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
6q9f
Structure name
aspartyl/asparaginyl beta-hydroxylase (asph) h679a in complex with mn, nog and factor x peptide fragment (39mer-4ser)
Structure deposition date
2018-12-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
10
% buried
88
Peptide accession
Q12797
Residue number A
660
Residue number B
685
Peptide name
Aspartyl/asparaginyl beta-hydroxylase
Ligandability
Cysteine 660 of Aspartyl/asparaginyl beta-hydroxylase
Cysteine 685 of Aspartyl/asparaginyl beta-hydroxylase
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