ERO1-like protein alpha
Intramolecular
Cysteine 94 and cysteine 131
Cysteine 35 and cysteine 48 L
Cysteine 37 and cysteine 46 L
Cysteine 208 and cysteine 241 L
Cysteine 85 and cysteine 391 L
Cysteine 394 and cysteine 397
Cysteine 46 and cysteine 48 L
Cysteine 37 and cysteine 48 L
Cysteine 35 and cysteine 37 L
Cysteine 35 and cysteine 46 L
3ahr A 94 A 131
A redox-regulated disulphide may form within ERO1-like protein alpha between cysteines 94 and 131.
Details
Redox score ?
94
PDB code
3ahr
Structure name
inactive human ero1
Structure deposition date
2010-04-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96HE7
Residue number A
94
Residue number B
131
Peptide name
ERO1-like protein alpha
Ligandability
Cysteine 94 of ERO1-like protein alpha
Cysteine 131 of ERO1-like protein alpha
3ahr A 35 A 48
A redox-regulated disulphide may form within ERO1-like protein alpha between cysteines 35 and 48.
Details
Redox score ?
89
PDB code
3ahr
Structure name
inactive human ero1
Structure deposition date
2010-04-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96HE7
Residue number A
35
Residue number B
48
Peptide name
ERO1-like protein alpha
Ligandability
Cysteine 35 of ERO1-like protein alpha
Cysteine 48 of ERO1-like protein alpha
3ahq A 37 A 46
A redox-regulated disulphide may form within ERO1-like protein alpha between cysteines 37 and 46.
Details
Redox score ?
87
PDB code
3ahq
Structure name
hyperactive human ero1
Structure deposition date
2010-04-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96HE7
Residue number A
37
Residue number B
46
Peptide name
ERO1-like protein alpha
Ligandability
Cysteine 37 of ERO1-like protein alpha
Cysteine 46 of ERO1-like protein alpha
3ahr A 208 A 241
A redox-regulated disulphide may form within ERO1-like protein alpha between cysteines 208 and 241.
Details
Redox score ?
85
PDB code
3ahr
Structure name
inactive human ero1
Structure deposition date
2010-04-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
39
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96HE7
Residue number A
208
Residue number B
241
Peptide name
ERO1-like protein alpha
Ligandability
Cysteine 208 of ERO1-like protein alpha
Cysteine 241 of ERO1-like protein alpha
3ahq A 85 A 391
A redox-regulated disulphide may form within ERO1-like protein alpha between cysteines 85 and 391.
Details
Redox score ?
84
PDB code
3ahq
Structure name
hyperactive human ero1
Structure deposition date
2010-04-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96HE7
Residue number A
85
Residue number B
391
Peptide name
ERO1-like protein alpha
Ligandability
Cysteine 85 of ERO1-like protein alpha
Cysteine 391 of ERO1-like protein alpha
3ahq A 394 A 397
A redox-regulated disulphide may form within ERO1-like protein alpha between cysteines 394 and 397.
Details
Redox score ?
79
PDB code
3ahq
Structure name
hyperactive human ero1
Structure deposition date
2010-04-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96HE7
Residue number A
394
Residue number B
397
Peptide name
ERO1-like protein alpha
Ligandability
Cysteine 394 of ERO1-like protein alpha
Cysteine 397 of ERO1-like protein alpha
3ahr A 46 A 48
A redox-regulated disulphide may form within ERO1-like protein alpha between cysteines 46 and 48.
Details
Redox score ?
61
PDB code
3ahr
Structure name
inactive human ero1
Structure deposition date
2010-04-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96HE7
Residue number A
46
Residue number B
48
Peptide name
ERO1-like protein alpha
Ligandability
Cysteine 46 of ERO1-like protein alpha
Cysteine 48 of ERO1-like protein alpha
3ahr A 37 A 48
A redox-regulated disulphide may form within ERO1-like protein alpha between cysteines 37 and 48.
Details
Redox score ?
61
PDB code
3ahr
Structure name
inactive human ero1
Structure deposition date
2010-04-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96HE7
Residue number A
37
Residue number B
48
Peptide name
ERO1-like protein alpha
Ligandability
Cysteine 37 of ERO1-like protein alpha
Cysteine 48 of ERO1-like protein alpha
3ahq A 35 A 37
A redox-regulated disulphide may form within ERO1-like protein alpha between cysteines 35 and 37. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
3ahq
Structure name
hyperactive human ero1
Structure deposition date
2010-04-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96HE7
Residue number A
35
Residue number B
37
Peptide name
ERO1-like protein alpha
Ligandability
Cysteine 35 of ERO1-like protein alpha
Cysteine 37 of ERO1-like protein alpha
3ahr A 35 A 46
A redox-regulated disulphide may form within ERO1-like protein alpha between cysteines 35 and 46. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
3ahr
Structure name
inactive human ero1
Structure deposition date
2010-04-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96HE7
Residue number A
35
Residue number B
46
Peptide name
ERO1-like protein alpha
Ligandability
Cysteine 35 of ERO1-like protein alpha
Cysteine 46 of ERO1-like protein alpha
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