Ubiquitin-like modifier-activating enzyme 5
Intermolecular
Cysteine 250 and cysteine 95
Intramolecular
Cysteine 226 and cysteine 308
Cysteine 229 and cysteine 308
Cysteine 229 and cysteine 303
Cysteine 303 and cysteine 308
Cysteine 226 and cysteine 229
Cysteine 195 and cysteine 226
Cysteine 226 and cysteine 303
5iaa A 250 B 95
A redox-regulated disulphide may form between two units of Ubiquitin-like modifier-activating enzyme 5 at cysteines 250 and 95. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
5iaa
Structure name
crystal structure of human uba5 in complex with ufm1
Structure deposition date
2016-02-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
68
Peptide A name
Ubiquitin-like modifier-activating enzyme 5
Peptide B name
Ubiquitin-like modifier-activating enzyme 5
Peptide A accession
Q9GZZ9
Peptide B accession
Q9GZZ9
Peptide A residue number
250
Peptide B residue number
95
Ligandability
Cysteine 250 of Ubiquitin-like modifier-activating enzyme 5
Cysteine 95 of Ubiquitin-like modifier-activating enzyme 5
6h78 N 226 N 308
A redox-regulated disulphide may form within Ubiquitin-like modifier-activating enzyme 5 between cysteines 226 and 308.
Details
Redox score ?
79
PDB code
6h78
Structure name
e1 enzyme for ubiquitin like protein activation
Structure deposition date
2018-07-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
87
Minimum pKa ?
6
% buried
68
Peptide accession
Q9GZZ9
Residue number A
226
Residue number B
308
Peptide name
Ubiquitin-like modifier-activating enzyme 5
Ligandability
Cysteine 226 of Ubiquitin-like modifier-activating enzyme 5
Cysteine 308 of Ubiquitin-like modifier-activating enzyme 5
6h77 D 229 D 308
A redox-regulated disulphide may form within Ubiquitin-like modifier-activating enzyme 5 between cysteines 229 and 308.
Details
Redox score ?
79
PDB code
6h77
Structure name
e1 enzyme for ubiquitin like protein activation in complex with ubl
Structure deposition date
2018-07-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
6
% buried
84
Peptide accession
Q9GZZ9
Residue number A
229
Residue number B
308
Peptide name
Ubiquitin-like modifier-activating enzyme 5
Ligandability
Cysteine 229 of Ubiquitin-like modifier-activating enzyme 5
Cysteine 308 of Ubiquitin-like modifier-activating enzyme 5
5iaa A 229 A 303
A redox-regulated disulphide may form within Ubiquitin-like modifier-activating enzyme 5 between cysteines 229 and 303.
Details
Redox score ?
78
PDB code
5iaa
Structure name
crystal structure of human uba5 in complex with ufm1
Structure deposition date
2016-02-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
6
% buried
86
Peptide accession
Q9GZZ9
Residue number A
229
Residue number B
303
Peptide name
Ubiquitin-like modifier-activating enzyme 5
Ligandability
Cysteine 229 of Ubiquitin-like modifier-activating enzyme 5
Cysteine 303 of Ubiquitin-like modifier-activating enzyme 5
6h78 A 303 A 308
A redox-regulated disulphide may form within Ubiquitin-like modifier-activating enzyme 5 between cysteines 303 and 308.
Details
Redox score ?
74
PDB code
6h78
Structure name
e1 enzyme for ubiquitin like protein activation
Structure deposition date
2018-07-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
46
Peptide accession
Q9GZZ9
Residue number A
303
Residue number B
308
Peptide name
Ubiquitin-like modifier-activating enzyme 5
Ligandability
Cysteine 303 of Ubiquitin-like modifier-activating enzyme 5
Cysteine 308 of Ubiquitin-like modifier-activating enzyme 5
6h77 B 226 B 229
A redox-regulated disulphide may form within Ubiquitin-like modifier-activating enzyme 5 between cysteines 226 and 229.
Details
Redox score ?
74
PDB code
6h77
Structure name
e1 enzyme for ubiquitin like protein activation in complex with ubl
Structure deposition date
2018-07-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
96
Minimum pKa ?
6
% buried
nan
Peptide accession
Q9GZZ9
Residue number A
226
Residue number B
229
Peptide name
Ubiquitin-like modifier-activating enzyme 5
Ligandability
Cysteine 226 of Ubiquitin-like modifier-activating enzyme 5
Cysteine 229 of Ubiquitin-like modifier-activating enzyme 5
6h78 L 195 L 226
A redox-regulated disulphide may form within Ubiquitin-like modifier-activating enzyme 5 between cysteines 195 and 226. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
6h78
Structure name
e1 enzyme for ubiquitin like protein activation
Structure deposition date
2018-07-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
90
Minimum pKa ?
0
% buried
88
Peptide accession
Q9GZZ9
Residue number A
195
Residue number B
226
Peptide name
Ubiquitin-like modifier-activating enzyme 5
Ligandability
Cysteine 195 of Ubiquitin-like modifier-activating enzyme 5
Cysteine 226 of Ubiquitin-like modifier-activating enzyme 5
5l95 A 226 A 303
A redox-regulated disulphide may form within Ubiquitin-like modifier-activating enzyme 5 between cysteines 226 and 303. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5l95
Structure name
crystal structure of human uba5 in complex with ufm1 and amp
Structure deposition date
2016-06-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
84
Minimum pKa ?
24
% buried
nan
Peptide accession
Q9GZZ9
Residue number A
226
Residue number B
303
Peptide name
Ubiquitin-like modifier-activating enzyme 5
Ligandability
Cysteine 226 of Ubiquitin-like modifier-activating enzyme 5
Cysteine 303 of Ubiquitin-like modifier-activating enzyme 5
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