Kelch-like protein 3
Intermolecular
Cysteine 526 and cysteine 549
Intramolecular
Cysteine 140 and cysteine 164
Cysteine 139 and cysteine 140
Cysteine 139 and cysteine 164
4ch9 A 526 B 549
A redox-regulated disulphide may form between two units of Kelch-like protein 3 at cysteines 526 and 549.
Details
Redox score ?
78
PDB code
4ch9
Structure name
crystal structure of the human klhl3 kelch domain in complex with a wnk4 peptide
Structure deposition date
2013-11-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide A name
Kelch-like protein 3
Peptide B name
Kelch-like protein 3
Peptide A accession
Q9UH77
Peptide B accession
Q9UH77
Peptide A residue number
526
Peptide B residue number
549
Ligandability
Cysteine 526 of Kelch-like protein 3
Cysteine 549 of Kelch-like protein 3
4hxi A 140 A 164
A redox-regulated disulphide may form within Kelch-like protein 3 between cysteines 140 and 164.
Details
Redox score ?
76
PDB code
4hxi
Structure name
crystal structure of klhl3/cul3 complex
Structure deposition date
2012-11-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
7
% buried
72
Peptide accession
Q9UH77
Residue number A
140
Residue number B
164
Peptide name
Kelch-like protein 3
Ligandability
Cysteine 140 of Kelch-like protein 3
Cysteine 164 of Kelch-like protein 3
4hxi A 139 A 140
A redox-regulated disulphide may form within Kelch-like protein 3 between cysteines 139 and 140. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
4hxi
Structure name
crystal structure of klhl3/cul3 complex
Structure deposition date
2012-11-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
65
Peptide accession
Q9UH77
Residue number A
139
Residue number B
140
Peptide name
Kelch-like protein 3
Ligandability
Cysteine 139 of Kelch-like protein 3
Cysteine 140 of Kelch-like protein 3
4hxi A 139 A 164
A redox-regulated disulphide may form within Kelch-like protein 3 between cysteines 139 and 164. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
4hxi
Structure name
crystal structure of klhl3/cul3 complex
Structure deposition date
2012-11-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
72
Peptide accession
Q9UH77
Residue number A
139
Residue number B
164
Peptide name
Kelch-like protein 3
Ligandability
Cysteine 139 of Kelch-like protein 3
Cysteine 164 of Kelch-like protein 3
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