DYNC2H1 variant protein
Intramolecular
Cysteine 2862 and cysteine 3225
Cysteine 1640 and cysteine 1641
Cysteine 4266 and cysteine 4288
Cysteine 3749 and cysteine 3770
Cysteine 2793 and cysteine 2803
Cysteine 2295 and cysteine 2497
Cysteine 3560 and cysteine 3562
Cysteine 1715 and cysteine 1739
6rla B 2862 B 3225
A redox-regulated disulphide may form within DYNC2H1 variant protein between cysteines 2862 and 3225.
Details
Redox score ?
62
PDB code
6rla
Structure name
structure of the dynein-2 complex; motor domains
Structure deposition date
2019-05-01
Thiol separation (Å)
6
Half-sphere exposure sum ?
50
Minimum pKa ?
10
% buried
35
Peptide accession
B0I1S0
Residue number A
2862
Residue number B
3225
Peptide name
DYNC2H1 variant protein
Ligandability
Cysteine 2862 of DYNC2H1 variant protein
Cysteine 3225 of DYNC2H1 variant protein
6rla A 1640 A 1641
A redox-regulated disulphide may form within DYNC2H1 variant protein between cysteines 1640 and 1641. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
6rla
Structure name
structure of the dynein-2 complex; motor domains
Structure deposition date
2019-05-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
11
% buried
52
Peptide accession
B0I1S0
Residue number A
1640
Residue number B
1641
Peptide name
DYNC2H1 variant protein
Ligandability
Cysteine 1640 of DYNC2H1 variant protein
Cysteine 1641 of DYNC2H1 variant protein
6rla A 4266 A 4288
A redox-regulated disulphide may form within DYNC2H1 variant protein between cysteines 4266 and 4288. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
6rla
Structure name
structure of the dynein-2 complex; motor domains
Structure deposition date
2019-05-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
26
Peptide accession
B0I1S0
Residue number A
4266
Residue number B
4288
Peptide name
DYNC2H1 variant protein
Ligandability
Cysteine 4266 of DYNC2H1 variant protein
Cysteine 4288 of DYNC2H1 variant protein
6rla B 3749 B 3770
A redox-regulated disulphide may form within DYNC2H1 variant protein between cysteines 3749 and 3770. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
6rla
Structure name
structure of the dynein-2 complex; motor domains
Structure deposition date
2019-05-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
18
Peptide accession
B0I1S0
Residue number A
3749
Residue number B
3770
Peptide name
DYNC2H1 variant protein
Ligandability
Cysteine 3749 of DYNC2H1 variant protein
Cysteine 3770 of DYNC2H1 variant protein
6rla B 2793 B 2803
A redox-regulated disulphide may form within DYNC2H1 variant protein between cysteines 2793 and 2803. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
6rla
Structure name
structure of the dynein-2 complex; motor domains
Structure deposition date
2019-05-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
84
Peptide accession
B0I1S0
Residue number A
2793
Residue number B
2803
Peptide name
DYNC2H1 variant protein
Ligandability
Cysteine 2793 of DYNC2H1 variant protein
Cysteine 2803 of DYNC2H1 variant protein
6rla B 2295 B 2497
A redox-regulated disulphide may form within DYNC2H1 variant protein between cysteines 2295 and 2497. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
6rla
Structure name
structure of the dynein-2 complex; motor domains
Structure deposition date
2019-05-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
77
Peptide accession
B0I1S0
Residue number A
2295
Residue number B
2497
Peptide name
DYNC2H1 variant protein
Ligandability
Cysteine 2295 of DYNC2H1 variant protein
Cysteine 2497 of DYNC2H1 variant protein
6rla A 3560 A 3562
A redox-regulated disulphide may form within DYNC2H1 variant protein between cysteines 3560 and 3562. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
6rla
Structure name
structure of the dynein-2 complex; motor domains
Structure deposition date
2019-05-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
96
Peptide accession
B0I1S0
Residue number A
3560
Residue number B
3562
Peptide name
DYNC2H1 variant protein
Ligandability
Cysteine 3560 of DYNC2H1 variant protein
Cysteine 3562 of DYNC2H1 variant protein
6rla A 1715 A 1739
A redox-regulated disulphide may form within DYNC2H1 variant protein between cysteines 1715 and 1739. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
6rla
Structure name
structure of the dynein-2 complex; motor domains
Structure deposition date
2019-05-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
100
Peptide accession
B0I1S0
Residue number A
1715
Residue number B
1739
Peptide name
DYNC2H1 variant protein
Ligandability
Cysteine 1715 of DYNC2H1 variant protein
Cysteine 1739 of DYNC2H1 variant protein
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