AP-1 complex subunit beta-1
Intramolecular
Cysteine 95 and cysteine 129
Cysteine 380 and cysteine 391
Cysteine 129 and cysteine 144
Cysteine 112 and cysteine 144
Cysteine 95 and cysteine 144
Cysteine 123 and cysteine 144
4hmy B 95 B 129
A redox-regulated disulphide may form within AP-1 complex subunit beta-1 between cysteines 95 and 129.
Details
Redox score ?
78
PDB code
4hmy
Structure name
structural basis for recruitment and activation of the ap-1 clathrin adaptor complex by arf1
Structure deposition date
2012-10-18
Thiol separation (Å)
3
Half-sphere exposure sum ?
76
Minimum pKa ?
9
% buried
91
Peptide accession
Q10567
Residue number A
95
Residue number B
129
Peptide name
AP-1 complex subunit beta-1
Ligandability
Cysteine 95 of AP-1 complex subunit beta-1
Cysteine 129 of AP-1 complex subunit beta-1
1w63 H 380 H 391
A redox-regulated disulphide may form within AP-1 complex subunit beta-1 between cysteines 380 and 391.
Details
Redox score ?
73
PDB code
1w63
Structure name
ap1 clathrin adaptor core
Structure deposition date
2004-08-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
8
% buried
72
Peptide accession
P52303
Residue number A
380
Residue number B
391
Peptide name
AP-1 complex subunit beta-1
Ligandability
Cysteine 380 of AP-1 complex subunit beta-1
Cysteine 391 of AP-1 complex subunit beta-1
1w63 H 129 H 144
A redox-regulated disulphide may form within AP-1 complex subunit beta-1 between cysteines 129 and 144. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
1w63
Structure name
ap1 clathrin adaptor core
Structure deposition date
2004-08-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
87
Minimum pKa ?
7
% buried
86
Peptide accession
P52303
Residue number A
129
Residue number B
144
Peptide name
AP-1 complex subunit beta-1
Ligandability
Cysteine 129 of AP-1 complex subunit beta-1
Cysteine 144 of AP-1 complex subunit beta-1
4p6z B 112 B 144
A redox-regulated disulphide may form within AP-1 complex subunit beta-1 between cysteines 112 and 144. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
4p6z
Structure name
crystal structure of the human bst2 cytoplasmic domain and the hiv-1 vpu cytoplasmic domain bound to the clathrin adaptor protein complex 1 (ap1) core
Structure deposition date
2014-03-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
92
Minimum pKa ?
10
% buried
100
Peptide accession
Q10567
Residue number A
112
Residue number B
144
Peptide name
AP-1 complex subunit beta-1
Ligandability
Cysteine 112 of AP-1 complex subunit beta-1
Cysteine 144 of AP-1 complex subunit beta-1
4hmy B 95 B 144
A redox-regulated disulphide may form within AP-1 complex subunit beta-1 between cysteines 95 and 144. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
4hmy
Structure name
structural basis for recruitment and activation of the ap-1 clathrin adaptor complex by arf1
Structure deposition date
2012-10-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
98
Peptide accession
Q10567
Residue number A
95
Residue number B
144
Peptide name
AP-1 complex subunit beta-1
Ligandability
Cysteine 95 of AP-1 complex subunit beta-1
Cysteine 144 of AP-1 complex subunit beta-1
4p6z B 123 B 144
A redox-regulated disulphide may form within AP-1 complex subunit beta-1 between cysteines 123 and 144. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
4p6z
Structure name
crystal structure of the human bst2 cytoplasmic domain and the hiv-1 vpu cytoplasmic domain bound to the clathrin adaptor protein complex 1 (ap1) core
Structure deposition date
2014-03-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
10
% buried
73
Peptide accession
Q10567
Residue number A
123
Residue number B
144
Peptide name
AP-1 complex subunit beta-1
Ligandability
Cysteine 123 of AP-1 complex subunit beta-1
Cysteine 144 of AP-1 complex subunit beta-1
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