Beta-catenin-like protein 1
4mfu A 318 A 320
A redox-regulated disulphide may form within Beta-catenin-like protein 1 between cysteines 318 and 320. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
4mfu
Structure name
crystal structure of human ctnnbl1(residues 77~563)
Structure deposition date
2013-08-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
100
Peptide accession
Q8WYA6
Residue number A
318
Residue number B
320
Peptide name
Beta-catenin-like protein 1
Ligandability
Cysteine 318 of Beta-catenin-like protein 1
Cysteine 320 of Beta-catenin-like protein 1
4mfu A 408 A 497
A redox-regulated disulphide may form within Beta-catenin-like protein 1 between cysteines 408 and 497. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
23
PDB code
4mfu
Structure name
crystal structure of human ctnnbl1(residues 77~563)
Structure deposition date
2013-08-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
13
% buried
100
Peptide accession
Q8WYA6
Residue number A
408
Residue number B
497
Peptide name
Beta-catenin-like protein 1
Ligandability
Cysteine 408 of Beta-catenin-like protein 1
Cysteine 497 of Beta-catenin-like protein 1
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