Ubiquitin-conjugating enzyme E2 Z
5a4p A 261 A 263
A redox-regulated disulphide may form within Ubiquitin-conjugating enzyme E2 Z between cysteines 261 and 263.
Details
Redox score ?
61
PDB code
5a4p
Structure name
structure of ube2z provides functional insight into specificity in the fat10 conjugation machinery
Structure deposition date
2015-06-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
57
Minimum pKa ?
11
% buried
58
Peptide accession
Q9H832
Residue number A
261
Residue number B
263
Peptide name
Ubiquitin-conjugating enzyme E2 Z
Ligandability
Cysteine 261 of Ubiquitin-conjugating enzyme E2 Z
Cysteine 263 of Ubiquitin-conjugating enzyme E2 Z
5a4p A 254 A 286
A redox-regulated disulphide may form within Ubiquitin-conjugating enzyme E2 Z between cysteines 254 and 286. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
5a4p
Structure name
structure of ube2z provides functional insight into specificity in the fat10 conjugation machinery
Structure deposition date
2015-06-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
84
Peptide accession
Q9H832
Residue number A
254
Residue number B
286
Peptide name
Ubiquitin-conjugating enzyme E2 Z
Ligandability
Cysteine 254 of Ubiquitin-conjugating enzyme E2 Z
Cysteine 286 of Ubiquitin-conjugating enzyme E2 Z
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