Kelch-like protein 7
Intramolecular
Cysteine 306 and cysteine 321
Cysteine 331 and cysteine 572
Cysteine 435 and cysteine 451
Cysteine 451 and cysteine 465
Cysteine 306 and cysteine 569
Cysteine 331 and cysteine 569
3ii7 A 306 A 321
A redox-regulated disulphide may form within Kelch-like protein 7 between cysteines 306 and 321.
Details
Redox score ?
77
PDB code
3ii7
Structure name
crystal structure of the kelch domain of human klhl7
Structure deposition date
2009-07-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
77
Peptide accession
Q8IXQ5
Residue number A
306
Residue number B
321
Peptide name
Kelch-like protein 7
Ligandability
Cysteine 306 of Kelch-like protein 7
Cysteine 321 of Kelch-like protein 7
3ii7 A 331 A 572
A redox-regulated disulphide may form within Kelch-like protein 7 between cysteines 331 and 572. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
3ii7
Structure name
crystal structure of the kelch domain of human klhl7
Structure deposition date
2009-07-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
84
Minimum pKa ?
13
% buried
100
Peptide accession
Q8IXQ5
Residue number A
331
Residue number B
572
Peptide name
Kelch-like protein 7
Ligandability
Cysteine 331 of Kelch-like protein 7
Cysteine 572 of Kelch-like protein 7
3ii7 A 435 A 451
A redox-regulated disulphide may form within Kelch-like protein 7 between cysteines 435 and 451. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
3ii7
Structure name
crystal structure of the kelch domain of human klhl7
Structure deposition date
2009-07-31
Thiol separation (Å)
5
Half-sphere exposure sum ?
95
Minimum pKa ?
12
% buried
100
Peptide accession
Q8IXQ5
Residue number A
435
Residue number B
451
Peptide name
Kelch-like protein 7
Ligandability
Cysteine 435 of Kelch-like protein 7
Cysteine 451 of Kelch-like protein 7
3ii7 A 451 A 465
A redox-regulated disulphide may form within Kelch-like protein 7 between cysteines 451 and 465. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
3ii7
Structure name
crystal structure of the kelch domain of human klhl7
Structure deposition date
2009-07-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
55
Peptide accession
Q8IXQ5
Residue number A
451
Residue number B
465
Peptide name
Kelch-like protein 7
Ligandability
Cysteine 451 of Kelch-like protein 7
Cysteine 465 of Kelch-like protein 7
3ii7 A 306 A 569
A redox-regulated disulphide may form within Kelch-like protein 7 between cysteines 306 and 569. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
3ii7
Structure name
crystal structure of the kelch domain of human klhl7
Structure deposition date
2009-07-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
8
% buried
92
Peptide accession
Q8IXQ5
Residue number A
306
Residue number B
569
Peptide name
Kelch-like protein 7
Ligandability
Cysteine 306 of Kelch-like protein 7
Cysteine 569 of Kelch-like protein 7
3ii7 A 331 A 569
A redox-regulated disulphide may form within Kelch-like protein 7 between cysteines 331 and 569. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
3ii7
Structure name
crystal structure of the kelch domain of human klhl7
Structure deposition date
2009-07-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
100
Peptide accession
Q8IXQ5
Residue number A
331
Residue number B
569
Peptide name
Kelch-like protein 7
Ligandability
Cysteine 331 of Kelch-like protein 7
Cysteine 569 of Kelch-like protein 7
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