AP-2 complex subunit beta
Intramolecular
Cysteine 95 and cysteine 129
Cysteine 380 and cysteine 391
Cysteine 112 and cysteine 144
Cysteine 129 and cysteine 144
Cysteine 95 and cysteine 123
Cysteine 95 and cysteine 144
Cysteine 123 and cysteine 144
2jkr E 95 E 129
A redox-regulated disulphide may form within AP-2 complex subunit beta between cysteines 95 and 129.
Details
Redox score ?
72
PDB code
2jkr
Structure name
ap2 clathrin adaptor core with dileucine peptide rm( phosphos)qikrllse
Structure deposition date
2008-08-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
8
% buried
82
Peptide accession
P63010
Residue number A
95
Residue number B
129
Peptide name
AP-2 complex subunit beta
Ligandability
Cysteine 95 of AP-2 complex subunit beta
Cysteine 129 of AP-2 complex subunit beta
6owt B 380 B 391
A redox-regulated disulphide may form within AP-2 complex subunit beta between cysteines 380 and 391. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
6owt
Structure name
structure of sivsmm nef and smm tetherin bound to the clathrin adaptor ap-2 complex
Structure deposition date
2019-05-10
Thiol separation (Å)
5
Half-sphere exposure sum ?
84
Minimum pKa ?
11
% buried
77
Peptide accession
P62944
Residue number A
380
Residue number B
391
Peptide name
AP-2 complex subunit beta
Ligandability
Cysteine 380 of AP-2 complex subunit beta
Cysteine 391 of AP-2 complex subunit beta
6owt B 112 B 144
A redox-regulated disulphide may form within AP-2 complex subunit beta 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 ?
50
PDB code
6owt
Structure name
structure of sivsmm nef and smm tetherin bound to the clathrin adaptor ap-2 complex
Structure deposition date
2019-05-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
94
Peptide accession
P62944
Residue number A
112
Residue number B
144
Peptide name
AP-2 complex subunit beta
Ligandability
Cysteine 112 of AP-2 complex subunit beta
Cysteine 144 of AP-2 complex subunit beta
7rw9 B 129 B 144
A redox-regulated disulphide may form within AP-2 complex subunit beta 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 ?
50
PDB code
7rw9
Structure name
ap2 bound to heparin in the bowl conformation
Structure deposition date
2021-08-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
10
% buried
64
Peptide accession
Q9DBG3
Residue number A
129
Residue number B
144
Peptide name
AP-2 complex subunit beta
Ligandability
Cysteine 129 of AP-2 complex subunit beta
Cysteine 144 of AP-2 complex subunit beta
6owo B 95 B 123
A redox-regulated disulphide may form within AP-2 complex subunit beta between cysteines 95 and 123. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
6owo
Structure name
cryo-em structure of phosphorylated ap-2 core bound to necap
Structure deposition date
2019-05-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
34
Peptide accession
Q9DBG3
Residue number A
95
Residue number B
123
Peptide name
AP-2 complex subunit beta
Ligandability
Cysteine 95 of AP-2 complex subunit beta
Cysteine 123 of AP-2 complex subunit beta
2jkt E 95 E 144
A redox-regulated disulphide may form within AP-2 complex subunit beta 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 ?
37
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)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
92
Peptide accession
P63010
Residue number A
95
Residue number B
144
Peptide name
AP-2 complex subunit beta
Ligandability
Cysteine 95 of AP-2 complex subunit beta
Cysteine 144 of AP-2 complex subunit beta
4uqi B 123 B 144
A redox-regulated disulphide may form within AP-2 complex subunit beta 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 ?
32
PDB code
4uqi
Structure name
ap2 controls clathrin polymerization with a membrane-activated switch
Structure deposition date
2014-06-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
69
Peptide accession
P63010
Residue number A
123
Residue number B
144
Peptide name
AP-2 complex subunit beta
Ligandability
Cysteine 123 of AP-2 complex subunit beta
Cysteine 144 of AP-2 complex subunit beta
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