AP-2 complex subunit alpha-2
2jkt A 492 A 533
A redox-regulated disulphide may form within AP-2 complex subunit alpha-2 between cysteines 491 and 532 (492 and 533 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
2jkt
Structure name
ap2 clathrin adaptor core with cd4 dileucine peptide rm( phosphos)eikrllse q to e mutant
Structure deposition date
2008-08-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
40
Peptide accession
P17427
Residue number A
491
Residue number B
532
Peptide name
AP-2 complex subunit alpha-2
Ligandability
Cysteine 491 of AP-2 complex subunit alpha-2
Cysteine 532 of AP-2 complex subunit alpha-2
2jkt L 134 L 171
A redox-regulated disulphide may form within AP-2 complex subunit alpha-2 between cysteines 134 and 171. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
2jkt
Structure name
ap2 clathrin adaptor core with cd4 dileucine peptide rm( phosphos)eikrllse q to e mutant
Structure deposition date
2008-08-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
94
Minimum pKa ?
12
% buried
100
Peptide accession
P17427
Residue number A
134
Residue number B
171
Peptide name
AP-2 complex subunit alpha-2
Ligandability
Cysteine 134 of AP-2 complex subunit alpha-2
Cysteine 171 of AP-2 complex subunit alpha-2
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