E3 ubiquitin-protein ligase Arkadia
Intramolecular
Cysteine 960 and cysteine 982
Cysteine 945 and cysteine 968
Cysteine 960 and cysteine 979
Cysteine 942 and cysteine 968
Cysteine 942 and cysteine 945
Cysteine 979 and cysteine 982
Cysteine 32 and cysteine 960
5lg0 A 35 A 57
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Arkadia between cysteines 960 and 982 (35 and 57 respectively in this structure).
Details
Redox score ?
87
PDB code
5lg0
Structure name
solution nmr structure of tryptophan to alanine mutant of arkadia ring domain
Structure deposition date
2016-07-05
Thiol separation (Å)
3
Half-sphere exposure sum ?
35
Minimum pKa ?
nan
% buried
0
Peptide accession
Q6ZNA4
Residue number A
960
Residue number B
982
Peptide name
E3 ubiquitin-protein ligase Arkadia
Ligandability
Cysteine 960 of E3 ubiquitin-protein ligase Arkadia
Cysteine 982 of E3 ubiquitin-protein ligase Arkadia
5lg0 A 20 A 43
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Arkadia between cysteines 945 and 968 (20 and 43 respectively in this structure).
Details
Redox score ?
83
PDB code
5lg0
Structure name
solution nmr structure of tryptophan to alanine mutant of arkadia ring domain
Structure deposition date
2016-07-05
Thiol separation (Å)
3
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
0
Peptide accession
Q6ZNA4
Residue number A
945
Residue number B
968
Peptide name
E3 ubiquitin-protein ligase Arkadia
Ligandability
Cysteine 945 of E3 ubiquitin-protein ligase Arkadia
Cysteine 968 of E3 ubiquitin-protein ligase Arkadia
5lg0 A 35 A 54
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Arkadia between cysteines 960 and 979 (35 and 54 respectively in this structure).
Details
Redox score ?
78
PDB code
5lg0
Structure name
solution nmr structure of tryptophan to alanine mutant of arkadia ring domain
Structure deposition date
2016-07-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
2
Peptide accession
Q6ZNA4
Residue number A
960
Residue number B
979
Peptide name
E3 ubiquitin-protein ligase Arkadia
Ligandability
Cysteine 960 of E3 ubiquitin-protein ligase Arkadia
Cysteine 979 of E3 ubiquitin-protein ligase Arkadia
7p2k A 17 A 43
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Arkadia between cysteines 942 and 968 (17 and 43 respectively in this structure).
Details
Redox score ?
77
PDB code
7p2k
Structure name
solution nmr structure of arginine to cysteine mutant of arkadia ring domain
Structure deposition date
2021-07-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
6
Peptide accession
Q6ZNA4
Residue number A
942
Residue number B
968
Peptide name
E3 ubiquitin-protein ligase Arkadia
Ligandability
Cysteine 942 of E3 ubiquitin-protein ligase Arkadia
Cysteine 968 of E3 ubiquitin-protein ligase Arkadia
5lg0 A 17 A 20
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Arkadia between cysteines 942 and 945 (17 and 20 respectively in this structure).
Details
Redox score ?
75
PDB code
5lg0
Structure name
solution nmr structure of tryptophan to alanine mutant of arkadia ring domain
Structure deposition date
2016-07-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
12
% buried
7
Peptide accession
Q6ZNA4
Residue number A
942
Residue number B
945
Peptide name
E3 ubiquitin-protein ligase Arkadia
Ligandability
Cysteine 942 of E3 ubiquitin-protein ligase Arkadia
Cysteine 945 of E3 ubiquitin-protein ligase Arkadia
5lg7 A 54 A 57
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Arkadia between cysteines 979 and 982 (54 and 57 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
5lg7
Structure name
solution nmr structure of tryptophan to arginine mutant of arkadia ring domain
Structure deposition date
2016-07-06
Thiol separation (Å)
3
Half-sphere exposure sum ?
37
Minimum pKa ?
35
% buried
0
Peptide accession
Q6ZNA4
Residue number A
979
Residue number B
982
Peptide name
E3 ubiquitin-protein ligase Arkadia
Ligandability
Cysteine 979 of E3 ubiquitin-protein ligase Arkadia
Cysteine 982 of E3 ubiquitin-protein ligase Arkadia
7p2k A 32 A 35
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase Arkadia between cysteines 32 and 960 (32 and 35 respectively in this structure).
Details
Redox score ?
nan
PDB code
7p2k
Structure name
solution nmr structure of arginine to cysteine mutant of arkadia ring domain
Structure deposition date
2021-07-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
8
Peptide accession
Q6ZNA4
Residue number A
32
Residue number B
960
Peptide name
E3 ubiquitin-protein ligase Arkadia
Ligandability
Cysteine 32 of E3 ubiquitin-protein ligase Arkadia
Cysteine 960 of E3 ubiquitin-protein ligase Arkadia
Cysteine 32 in protein A could not be asigned to a Uniprot residue.
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