Kinesin-1 heavy chain
Intramolecular
Cysteine 13 and cysteine 302
Cysteine 301 and cysteine 302
Cysteine 7 and cysteine 294 L
Cysteine 13 and cysteine 301
Cysteine 65 and cysteine 301 L
5lt3 B 13 B 302
A redox-regulated disulphide may form within Kinesin-1 heavy chain between cysteines 13 and 302.
Details
Redox score ?
64
PDB code
5lt3
Structure name
nucleotide-free kinesin-1 motor domain t87a mutant, p1 crystal form
Structure deposition date
2016-09-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
97
Minimum pKa ?
9
% buried
100
Peptide accession
P33176
Residue number A
13
Residue number B
302
Peptide name
Kinesin-1 heavy chain
Ligandability
Cysteine 13 of Kinesin-1 heavy chain
Cysteine 302 of Kinesin-1 heavy chain
4atx C 301 C 302
A redox-regulated disulphide may form within Kinesin-1 heavy chain between cysteines 301 and 302. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
4atx
Structure name
rigor kinesin motor domain with an ordered neck-linker, docked on tubulin dimer, modelled into the 8a cryo-em map of doublecortin- microtubules decorated with kinesin
Structure deposition date
2012-05-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
90
Minimum pKa ?
9
% buried
100
Peptide accession
Q2PQA9
Residue number A
301
Residue number B
302
Peptide name
Kinesin-1 heavy chain
Ligandability
Cysteine 301 of Kinesin-1 heavy chain
Cysteine 302 of Kinesin-1 heavy chain
1mkj A 7 A 294
A redox-regulated disulphide may form within Kinesin-1 heavy chain between cysteines 7 and 294. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
1mkj
Structure name
human kinesin motor domain with docked neck linker
Structure deposition date
2002-08-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
68
Peptide accession
P33176
Residue number A
7
Residue number B
294
Peptide name
Kinesin-1 heavy chain
Ligandability
Cysteine 7 of Kinesin-1 heavy chain
Cysteine 294 of Kinesin-1 heavy chain
4atx C 13 C 301
A redox-regulated disulphide may form within Kinesin-1 heavy chain between cysteines 13 and 301. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
4atx
Structure name
rigor kinesin motor domain with an ordered neck-linker, docked on tubulin dimer, modelled into the 8a cryo-em map of doublecortin- microtubules decorated with kinesin
Structure deposition date
2012-05-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
94
Minimum pKa ?
11
% buried
100
Peptide accession
Q2PQA9
Residue number A
13
Residue number B
301
Peptide name
Kinesin-1 heavy chain
Ligandability
Cysteine 13 of Kinesin-1 heavy chain
Cysteine 301 of Kinesin-1 heavy chain
4atx C 65 C 301
A redox-regulated disulphide may form within Kinesin-1 heavy chain between cysteines 65 and 301. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
4atx
Structure name
rigor kinesin motor domain with an ordered neck-linker, docked on tubulin dimer, modelled into the 8a cryo-em map of doublecortin- microtubules decorated with kinesin
Structure deposition date
2012-05-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
11
% buried
100
Peptide accession
Q2PQA9
Residue number A
65
Residue number B
301
Peptide name
Kinesin-1 heavy chain
Ligandability
Cysteine 65 of Kinesin-1 heavy chain
Cysteine 301 of Kinesin-1 heavy chain
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