Cytoplasmic polyadenylation element-binding protein 1
Intramolecular
Cysteine 518 and cysteine 537
Cysteine 518 and cysteine 540
Cysteine 527 and cysteine 532
Cysteine 537 and cysteine 540
Cysteine 515 and cysteine 518
Cysteine 515 and cysteine 540
Cysteine 515 and cysteine 537
Cysteine 532 and cysteine 540
2mke A 438 A 457
A redox-regulated disulphide may form within Cytoplasmic polyadenylation element-binding protein 1 between cysteines 518 and 537 (438 and 457 respectively in this structure).
Details
Redox score ?
82
PDB code
2mke
Structure name
solution structure of cpeb1 zz domain in the free state
Structure deposition date
2014-02-06
Thiol separation (Å)
3
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
2
Peptide accession
Q9BZB8
Residue number A
518
Residue number B
537
Peptide name
Cytoplasmic polyadenylation element-binding protein 1
Ligandability
Cysteine 518 of Cytoplasmic polyadenylation element-binding protein 1
Cysteine 537 of Cytoplasmic polyadenylation element-binding protein 1
2mke A 438 A 460
A redox-regulated disulphide may form within Cytoplasmic polyadenylation element-binding protein 1 between cysteines 518 and 540 (438 and 460 respectively in this structure).
Details
Redox score ?
82
PDB code
2mke
Structure name
solution structure of cpeb1 zz domain in the free state
Structure deposition date
2014-02-06
Thiol separation (Å)
3
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
7
Peptide accession
Q9BZB8
Residue number A
518
Residue number B
540
Peptide name
Cytoplasmic polyadenylation element-binding protein 1
Ligandability
Cysteine 518 of Cytoplasmic polyadenylation element-binding protein 1
Cysteine 540 of Cytoplasmic polyadenylation element-binding protein 1
2mke A 447 A 452
A redox-regulated disulphide may form within Cytoplasmic polyadenylation element-binding protein 1 between cysteines 527 and 532 (447 and 452 respectively in this structure).
Details
Redox score ?
81
PDB code
2mke
Structure name
solution structure of cpeb1 zz domain in the free state
Structure deposition date
2014-02-06
Thiol separation (Å)
3
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9BZB8
Residue number A
527
Residue number B
532
Peptide name
Cytoplasmic polyadenylation element-binding protein 1
Ligandability
Cysteine 527 of Cytoplasmic polyadenylation element-binding protein 1
Cysteine 532 of Cytoplasmic polyadenylation element-binding protein 1
2mke A 457 A 460
A redox-regulated disulphide may form within Cytoplasmic polyadenylation element-binding protein 1 between cysteines 537 and 540 (457 and 460 respectively in this structure).
Details
Redox score ?
81
PDB code
2mke
Structure name
solution structure of cpeb1 zz domain in the free state
Structure deposition date
2014-02-06
Thiol separation (Å)
3
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
8
Peptide accession
Q9BZB8
Residue number A
537
Residue number B
540
Peptide name
Cytoplasmic polyadenylation element-binding protein 1
Ligandability
Cysteine 537 of Cytoplasmic polyadenylation element-binding protein 1
Cysteine 540 of Cytoplasmic polyadenylation element-binding protein 1
2mke A 435 A 438
A redox-regulated disulphide may form within Cytoplasmic polyadenylation element-binding protein 1 between cysteines 515 and 518 (435 and 438 respectively in this structure).
Details
Redox score ?
80
PDB code
2mke
Structure name
solution structure of cpeb1 zz domain in the free state
Structure deposition date
2014-02-06
Thiol separation (Å)
3
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9BZB8
Residue number A
515
Residue number B
518
Peptide name
Cytoplasmic polyadenylation element-binding protein 1
Ligandability
Cysteine 515 of Cytoplasmic polyadenylation element-binding protein 1
Cysteine 518 of Cytoplasmic polyadenylation element-binding protein 1
2mke A 435 A 460
A redox-regulated disulphide may form within Cytoplasmic polyadenylation element-binding protein 1 between cysteines 515 and 540 (435 and 460 respectively in this structure).
Details
Redox score ?
79
PDB code
2mke
Structure name
solution structure of cpeb1 zz domain in the free state
Structure deposition date
2014-02-06
Thiol separation (Å)
3
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9BZB8
Residue number A
515
Residue number B
540
Peptide name
Cytoplasmic polyadenylation element-binding protein 1
Ligandability
Cysteine 515 of Cytoplasmic polyadenylation element-binding protein 1
Cysteine 540 of Cytoplasmic polyadenylation element-binding protein 1
2mke A 435 A 457
A redox-regulated disulphide may form within Cytoplasmic polyadenylation element-binding protein 1 between cysteines 515 and 537 (435 and 457 respectively in this structure).
Details
Redox score ?
79
PDB code
2mke
Structure name
solution structure of cpeb1 zz domain in the free state
Structure deposition date
2014-02-06
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
8
% buried
nan
Peptide accession
Q9BZB8
Residue number A
515
Residue number B
537
Peptide name
Cytoplasmic polyadenylation element-binding protein 1
Ligandability
Cysteine 515 of Cytoplasmic polyadenylation element-binding protein 1
Cysteine 537 of Cytoplasmic polyadenylation element-binding protein 1
2mke A 452 A 460
A redox-regulated disulphide may form within Cytoplasmic polyadenylation element-binding protein 1 between cysteines 532 and 540 (452 and 460 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
2mke
Structure name
solution structure of cpeb1 zz domain in the free state
Structure deposition date
2014-02-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9BZB8
Residue number A
532
Residue number B
540
Peptide name
Cytoplasmic polyadenylation element-binding protein 1
Ligandability
Cysteine 532 of Cytoplasmic polyadenylation element-binding protein 1
Cysteine 540 of Cytoplasmic polyadenylation element-binding protein 1
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