Kinesin heavy chain isoform 5C
Intramolecular
Cysteine 13 and cysteine 304
Cysteine 303 and cysteine 304
Cysteine 7 and cysteine 296
Cysteine 13 and cysteine 303
Cysteine 66 and cysteine 303
3wrd A 13 A 304
A redox-regulated disulphide may form within Kinesin heavy chain isoform 5C between cysteines 13 and 304.
Details
Redox score ?
63
PDB code
3wrd
Structure name
crystal structure of the kif5c motor domain without any nucleotide
Structure deposition date
2014-02-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
97
Minimum pKa ?
9
% buried
100
Peptide accession
P28738
Residue number A
13
Residue number B
304
Peptide name
Kinesin heavy chain isoform 5C
Ligandability
Cysteine 13 of Kinesin heavy chain isoform 5C
Cysteine 304 of Kinesin heavy chain isoform 5C
3wrd B 303 B 304
A redox-regulated disulphide may form within Kinesin heavy chain isoform 5C between cysteines 303 and 304. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
3wrd
Structure name
crystal structure of the kif5c motor domain without any nucleotide
Structure deposition date
2014-02-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
94
Minimum pKa ?
9
% buried
100
Peptide accession
P28738
Residue number A
303
Residue number B
304
Peptide name
Kinesin heavy chain isoform 5C
Ligandability
Cysteine 303 of Kinesin heavy chain isoform 5C
Cysteine 304 of Kinesin heavy chain isoform 5C
3x2t A 7 A 296
A redox-regulated disulphide may form within Kinesin heavy chain isoform 5C between cysteines 7 and 296. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
3x2t
Structure name
crystal structure of the kif5c motor domain with adp
Structure deposition date
2015-01-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
64
Peptide accession
P28738
Residue number A
7
Residue number B
296
Peptide name
Kinesin heavy chain isoform 5C
Ligandability
Cysteine 7 of Kinesin heavy chain isoform 5C
Cysteine 296 of Kinesin heavy chain isoform 5C
3wrd A 13 A 303
A redox-regulated disulphide may form within Kinesin heavy chain isoform 5C between cysteines 13 and 303. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
3wrd
Structure name
crystal structure of the kif5c motor domain without any nucleotide
Structure deposition date
2014-02-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
93
Minimum pKa ?
12
% buried
100
Peptide accession
P28738
Residue number A
13
Residue number B
303
Peptide name
Kinesin heavy chain isoform 5C
Ligandability
Cysteine 13 of Kinesin heavy chain isoform 5C
Cysteine 303 of Kinesin heavy chain isoform 5C
3x2t A 66 A 303
A redox-regulated disulphide may form within Kinesin heavy chain isoform 5C between cysteines 66 and 303. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
3x2t
Structure name
crystal structure of the kif5c motor domain with adp
Structure deposition date
2015-01-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
100
Peptide accession
P28738
Residue number A
66
Residue number B
303
Peptide name
Kinesin heavy chain isoform 5C
Ligandability
Cysteine 66 of Kinesin heavy chain isoform 5C
Cysteine 303 of Kinesin heavy chain isoform 5C
If this tool was useful for finding a disulphide, please cite: