Diphthamide biosynthesis protein 3
Intramolecular
Cysteine 26 and cysteine 48
Cysteine 26 and cysteine 28
Cysteine 28 and cysteine 48
Cysteine 28 and cysteine 51
Cysteine 48 and cysteine 51
Cysteine 26 and cysteine 51
1wge A 33 A 55
A redox-regulated disulphide may form within Diphthamide biosynthesis protein 3 between cysteines 26 and 48 (33 and 55 respectively in this structure).
Details
Redox score ?
90
PDB code
1wge
Structure name
solution structure of the mouse desr1
Structure deposition date
2004-05-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
0
Peptide accession
Q8K0W9
Residue number A
26
Residue number B
48
Peptide name
Diphthamide biosynthesis protein 3
Ligandability
Cysteine 26 of Diphthamide biosynthesis protein 3
Cysteine 48 of Diphthamide biosynthesis protein 3
2jr7 A 26 A 28
A redox-regulated disulphide may form within Diphthamide biosynthesis protein 3 between cysteines 26 and 28.
Details
Redox score ?
88
PDB code
2jr7
Structure name
solution structure of human desr1
Structure deposition date
2007-06-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
6
% buried
0
Peptide accession
Q96FX2
Residue number A
26
Residue number B
28
Peptide name
Diphthamide biosynthesis protein 3
Ligandability
Cysteine 26 of Diphthamide biosynthesis protein 3
Cysteine 28 of Diphthamide biosynthesis protein 3
2jr7 A 28 A 48
A redox-regulated disulphide may form within Diphthamide biosynthesis protein 3 between cysteines 28 and 48.
Details
Redox score ?
88
PDB code
2jr7
Structure name
solution structure of human desr1
Structure deposition date
2007-06-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
6
% buried
0
Peptide accession
Q96FX2
Residue number A
28
Residue number B
48
Peptide name
Diphthamide biosynthesis protein 3
Ligandability
Cysteine 28 of Diphthamide biosynthesis protein 3
Cysteine 48 of Diphthamide biosynthesis protein 3
2jr7 A 28 A 51
A redox-regulated disulphide may form within Diphthamide biosynthesis protein 3 between cysteines 28 and 51.
Details
Redox score ?
86
PDB code
2jr7
Structure name
solution structure of human desr1
Structure deposition date
2007-06-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
32
Minimum pKa ?
6
% buried
0
Peptide accession
Q96FX2
Residue number A
28
Residue number B
51
Peptide name
Diphthamide biosynthesis protein 3
Ligandability
Cysteine 28 of Diphthamide biosynthesis protein 3
Cysteine 51 of Diphthamide biosynthesis protein 3
1wge A 55 A 58
A redox-regulated disulphide may form within Diphthamide biosynthesis protein 3 between cysteines 48 and 51 (55 and 58 respectively in this structure).
Details
Redox score ?
85
PDB code
1wge
Structure name
solution structure of the mouse desr1
Structure deposition date
2004-05-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
6
% buried
0
Peptide accession
Q8K0W9
Residue number A
48
Residue number B
51
Peptide name
Diphthamide biosynthesis protein 3
Ligandability
Cysteine 48 of Diphthamide biosynthesis protein 3
Cysteine 51 of Diphthamide biosynthesis protein 3
1wge A 33 A 58
A redox-regulated disulphide may form within Diphthamide biosynthesis protein 3 between cysteines 26 and 51 (33 and 58 respectively in this structure).
Details
Redox score ?
82
PDB code
1wge
Structure name
solution structure of the mouse desr1
Structure deposition date
2004-05-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
10
% buried
0
Peptide accession
Q8K0W9
Residue number A
26
Residue number B
51
Peptide name
Diphthamide biosynthesis protein 3
Ligandability
Cysteine 26 of Diphthamide biosynthesis protein 3
Cysteine 51 of Diphthamide biosynthesis protein 3
If this tool was useful for finding a disulphide, please cite: