AP-1 complex subunit gamma-1
Intramolecular
Cysteine 392 and cysteine 400
Cysteine 124 and cysteine 128
Cysteine 492 and cysteine 539
Cysteine 128 and cysteine 160
Cysteine 135 and cysteine 160
Cysteine 124 and cysteine 160
Cysteine 47 and cysteine 70
4hmy A 392 A 400
A redox-regulated disulphide may form within AP-1 complex subunit gamma-1 between cysteines 392 and 400.
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)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
8
% buried
68
Peptide accession
P22892
Residue number A
392
Residue number B
400
Peptide name
AP-1 complex subunit gamma-1
Ligandability
Cysteine 392 of AP-1 complex subunit gamma-1
Cysteine 400 of AP-1 complex subunit gamma-1
4p6z G 124 G 128
A redox-regulated disulphide may form within AP-1 complex subunit gamma-1 between cysteines 124 and 128.
Details
Redox score ?
65
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)
4
Half-sphere exposure sum ?
94
Minimum pKa ?
7
% buried
100
Peptide accession
P22892
Residue number A
124
Residue number B
128
Peptide name
AP-1 complex subunit gamma-1
Ligandability
Cysteine 124 of AP-1 complex subunit gamma-1
Cysteine 128 of AP-1 complex subunit gamma-1
6d83 G 492 G 539
A redox-regulated disulphide may form within AP-1 complex subunit gamma-1 between cysteines 492 and 539. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
6d83
Structure name
structure of the cargo bound ap-1:arf1:tetherin-nef (l164a, l165a) dileucine mutant dimer monomeric subunit
Structure deposition date
2018-04-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
43
Minimum pKa ?
9
% buried
17
Peptide accession
P22892
Residue number A
492
Residue number B
539
Peptide name
AP-1 complex subunit gamma-1
Ligandability
Cysteine 492 of AP-1 complex subunit gamma-1
Cysteine 539 of AP-1 complex subunit gamma-1
4p6z G 128 G 160
A redox-regulated disulphide may form within AP-1 complex subunit gamma-1 between cysteines 128 and 160. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
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 ?
101
Minimum pKa ?
7
% buried
100
Peptide accession
P22892
Residue number A
128
Residue number B
160
Peptide name
AP-1 complex subunit gamma-1
Ligandability
Cysteine 128 of AP-1 complex subunit gamma-1
Cysteine 160 of AP-1 complex subunit gamma-1
1w63 G 135 G 160
A redox-regulated disulphide may form within AP-1 complex subunit gamma-1 between cysteines 135 and 160. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
1w63
Structure name
ap1 clathrin adaptor core
Structure deposition date
2004-08-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
11
% buried
86
Peptide accession
P22892
Residue number A
135
Residue number B
160
Peptide name
AP-1 complex subunit gamma-1
Ligandability
Cysteine 135 of AP-1 complex subunit gamma-1
Cysteine 160 of AP-1 complex subunit gamma-1
4hmy A 124 A 160
A redox-regulated disulphide may form within AP-1 complex subunit gamma-1 between cysteines 124 and 160. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
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 ?
102
Minimum pKa ?
13
% buried
100
Peptide accession
P22892
Residue number A
124
Residue number B
160
Peptide name
AP-1 complex subunit gamma-1
Ligandability
Cysteine 124 of AP-1 complex subunit gamma-1
Cysteine 160 of AP-1 complex subunit gamma-1
7r4h G 47 G 70
A redox-regulated disulphide may form within AP-1 complex subunit gamma-1 between cysteines 47 and 70. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
26
PDB code
7r4h
Structure name
phospho-sting binding to adaptor protein complex-1
Structure deposition date
2022-02-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
90
Peptide accession
P22892
Residue number A
47
Residue number B
70
Peptide name
AP-1 complex subunit gamma-1
Ligandability
Cysteine 47 of AP-1 complex subunit gamma-1
Cysteine 70 of AP-1 complex subunit gamma-1
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