Aspartoacylase
Intramolecular
Cysteine 310 and cysteine 311
Cysteine 124 and cysteine 152
Cysteine 145 and cysteine 151
4mri A 310 A 311
A redox-regulated disulphide may form within Aspartoacylase between cysteines 310 and 311.
Details
Redox score ?
72
PDB code
4mri
Structure name
human brain aspartoacylase mutant f295s complex with intermediate analog (n-phosphonomethyl-l-aspartate)
Structure deposition date
2013-09-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
1
Peptide accession
P45381
Residue number A
310
Residue number B
311
Peptide name
Aspartoacylase
Ligandability
Cysteine 310 of Aspartoacylase
Cysteine 311 of Aspartoacylase
2i3c A 124 A 152
A redox-regulated disulphide may form within Aspartoacylase between cysteines 124 and 152. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
2i3c
Structure name
crystal structure of an aspartoacylase from homo sapiens
Structure deposition date
2006-08-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
82
Peptide accession
P45381
Residue number A
124
Residue number B
152
Peptide name
Aspartoacylase
Ligandability
Cysteine 124 of Aspartoacylase
Cysteine 152 of Aspartoacylase
2gu2 A 145 A 151
A redox-regulated disulphide may form within Aspartoacylase between cysteines 145 and 151. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
2gu2
Structure name
crystal structure of an aspartoacylase from rattus norvegicus
Structure deposition date
2006-04-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
60
Peptide accession
Q9R1T5
Residue number A
145
Residue number B
151
Peptide name
Aspartoacylase
Ligandability
Cysteine 145 of Aspartoacylase
Cysteine 151 of Aspartoacylase
If this tool was useful for finding a disulphide, please cite: