Pleckstrin homology domain-containing family B member 2
Intramolecular
Cysteine 53 and cysteine 81
Cysteine 75 and cysteine 90
Cysteine 75 and cysteine 97
Cysteine 62 and cysteine 97
Cysteine 90 and cysteine 97
Cysteine 62 and cysteine 90
Cysteine 62 and cysteine 75
3aj4 B 53 B 81
A redox-regulated disulphide may form within Pleckstrin homology domain-containing family B member 2 between cysteines 53 and 81.
Details
Redox score ?
64
PDB code
3aj4
Structure name
crystal structure of the ph domain of evectin-2 from human complexed with o-phospho-l-serine
Structure deposition date
2010-05-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
53
Minimum pKa ?
11
% buried
50
Peptide accession
Q96CS7
Residue number A
53
Residue number B
81
Peptide name
Pleckstrin homology domain-containing family B member 2
Ligandability
Cysteine 53 of Pleckstrin homology domain-containing family B member 2
Cysteine 81 of Pleckstrin homology domain-containing family B member 2
3via B 77 B 92
A redox-regulated disulphide may form within Pleckstrin homology domain-containing family B member 2 between cysteines 75 and 90 (77 and 92 respectively in this structure).
Details
Redox score ?
63
PDB code
3via
Structure name
crystal structure of the ph domain of evectin-2 from human
Structure deposition date
2011-09-26
Thiol separation (Å)
5
Half-sphere exposure sum ?
80
Minimum pKa ?
9
% buried
31
Peptide accession
Q96CS7
Residue number A
75
Residue number B
90
Peptide name
Pleckstrin homology domain-containing family B member 2
Ligandability
Cysteine 75 of Pleckstrin homology domain-containing family B member 2
Cysteine 90 of Pleckstrin homology domain-containing family B member 2
3via A 77 A 99
A redox-regulated disulphide may form within Pleckstrin homology domain-containing family B member 2 between cysteines 75 and 97 (77 and 99 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
3via
Structure name
crystal structure of the ph domain of evectin-2 from human
Structure deposition date
2011-09-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
30
Peptide accession
Q96CS7
Residue number A
75
Residue number B
97
Peptide name
Pleckstrin homology domain-containing family B member 2
Ligandability
Cysteine 75 of Pleckstrin homology domain-containing family B member 2
Cysteine 97 of Pleckstrin homology domain-containing family B member 2
3aj4 A 62 A 97
A redox-regulated disulphide may form within Pleckstrin homology domain-containing family B member 2 between cysteines 62 and 97. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
3aj4
Structure name
crystal structure of the ph domain of evectin-2 from human complexed with o-phospho-l-serine
Structure deposition date
2010-05-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
56
Minimum pKa ?
11
% buried
51
Peptide accession
Q96CS7
Residue number A
62
Residue number B
97
Peptide name
Pleckstrin homology domain-containing family B member 2
Ligandability
Cysteine 62 of Pleckstrin homology domain-containing family B member 2
Cysteine 97 of Pleckstrin homology domain-containing family B member 2
2dhi A 95 A 102
A redox-regulated disulphide may form within Pleckstrin homology domain-containing family B member 2 between cysteines 90 and 97 (95 and 102 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
2dhi
Structure name
solution structure of the ph domain of evectin-2 from mouse
Structure deposition date
2006-03-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
52
Peptide accession
Q9QZC7
Residue number A
90
Residue number B
97
Peptide name
Pleckstrin homology domain-containing family B member 2
Ligandability
Cysteine 90 of Pleckstrin homology domain-containing family B member 2
Cysteine 97 of Pleckstrin homology domain-containing family B member 2
3via A 64 A 92
A redox-regulated disulphide may form within Pleckstrin homology domain-containing family B member 2 between cysteines 62 and 90 (64 and 92 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
3via
Structure name
crystal structure of the ph domain of evectin-2 from human
Structure deposition date
2011-09-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
46
Peptide accession
Q96CS7
Residue number A
62
Residue number B
90
Peptide name
Pleckstrin homology domain-containing family B member 2
Ligandability
Cysteine 62 of Pleckstrin homology domain-containing family B member 2
Cysteine 90 of Pleckstrin homology domain-containing family B member 2
2dhi A 67 A 80
A redox-regulated disulphide may form within Pleckstrin homology domain-containing family B member 2 between cysteines 62 and 75 (67 and 80 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
2dhi
Structure name
solution structure of the ph domain of evectin-2 from mouse
Structure deposition date
2006-03-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
34
Peptide accession
Q9QZC7
Residue number A
62
Residue number B
75
Peptide name
Pleckstrin homology domain-containing family B member 2
Ligandability
Cysteine 62 of Pleckstrin homology domain-containing family B member 2
Cysteine 75 of Pleckstrin homology domain-containing family B member 2
If this tool was useful for finding a disulphide, please cite: