Kinesin light chain 2
Intermolecular
Cysteine 221 and cysteine 221 L
Intramolecular
Cysteine 441 and cysteine 474 L
Cysteine 305 and cysteine 334
Cysteine 334 and cysteine 375
3ceq A 221 B 221
A redox-regulated disulphide may form between two units of Kinesin light chain 2 at cysteines 221 and 221. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
3ceq
Structure name
the tpr domain of human kinesin light chain 2 (hklc2)
Structure deposition date
2008-02-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
92
Peptide A name
Kinesin light chain 2
Peptide B name
Kinesin light chain 2
Peptide A accession
Q9H0B6
Peptide B accession
Q9H0B6
Peptide A residue number
221
Peptide B residue number
221
Ligandability
3edt B 441 B 474
A redox-regulated disulphide may form within Kinesin light chain 2 between cysteines 441 and 474.
Details
Redox score ?
75
PDB code
3edt
Structure name
crystal structure of the mutated s328n hklc2 tpr domain
Structure deposition date
2008-09-03
Thiol separation (Å)
3
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H0B6
Residue number A
441
Residue number B
474
Peptide name
Kinesin light chain 2
Ligandability
Cysteine 441 of Kinesin light chain 2
Cysteine 474 of Kinesin light chain 2
3ceq A 305 A 334
A redox-regulated disulphide may form within Kinesin light chain 2 between cysteines 305 and 334. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
3ceq
Structure name
the tpr domain of human kinesin light chain 2 (hklc2)
Structure deposition date
2008-02-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
60
Peptide accession
Q9H0B6
Residue number A
305
Residue number B
334
Peptide name
Kinesin light chain 2
Ligandability
Cysteine 305 of Kinesin light chain 2
Cysteine 334 of Kinesin light chain 2
3edt B 334 B 375
A redox-regulated disulphide may form within Kinesin light chain 2 between cysteines 334 and 375. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
3edt
Structure name
crystal structure of the mutated s328n hklc2 tpr domain
Structure deposition date
2008-09-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H0B6
Residue number A
334
Residue number B
375
Peptide name
Kinesin light chain 2
Ligandability
Cysteine 334 of Kinesin light chain 2
Cysteine 375 of Kinesin light chain 2
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