ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cytoplasmic dynein 1 heavy chain 1

Intramolecular
Cysteine 1977 and cysteine 1999 L
Cysteine 2985 and cysteine 3033 L
Cysteine 2594 and cysteine 2712
Cysteine 3712 and cysteine 3808 L
Cysteine 1949 and cysteine 1999 L
Cysteine 4510 and cysteine 4644
Cysteine 3323 and cysteine 3387
Cysteine 1949 and cysteine 1977
Cysteine 2663 and cysteine 2712
Cysteine 1888 and cysteine 1956 L
Cysteine 1932 and cysteine 1956
A redox-regulated disulphide may form within Cytoplasmic dynein 1 heavy chain 1 between cysteines 1977 and 1999.

Details

Redox score ?
78
PDB code
8dyv
Structure name
structure of human cytoplasmic dynein-1 bound to one lis1
Structure deposition date
2022-08-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
7
% buried
54
Peptide accession
Q14204
Residue number A
1977
Residue number B
1999
Peptide name
Cytoplasmic dynein 1 heavy chain 1

Ligandability

Cysteine 1977 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1999 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Cytoplasmic dynein 1 heavy chain 1 between cysteines 2985 and 3033.

Details

Redox score ?
75
PDB code
5nug
Structure name
motor domains from human cytoplasmic dynein-1 in the phi-particle conformation
Structure deposition date
2017-04-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
77
Minimum pKa ?
8
% buried
78
Peptide accession
Q14204
Residue number A
2985
Residue number B
3033
Peptide name
Cytoplasmic dynein 1 heavy chain 1

Ligandability

Cysteine 2985 of Cytoplasmic dynein 1 heavy chain 1

Ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 3033 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Cytoplasmic dynein 1 heavy chain 1 between cysteines 2594 and 2712.

Details

Redox score ?
67
PDB code
5nug
Structure name
motor domains from human cytoplasmic dynein-1 in the phi-particle conformation
Structure deposition date
2017-04-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
89
Minimum pKa ?
9
% buried
100
Peptide accession
Q14204
Residue number A
2594
Residue number B
2712
Peptide name
Cytoplasmic dynein 1 heavy chain 1

Ligandability

Cysteine 2594 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2712 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Cytoplasmic dynein 1 heavy chain 1 between cysteines 3712 and 3808.

Details

Redox score ?
65
PDB code
5nug
Structure name
motor domains from human cytoplasmic dynein-1 in the phi-particle conformation
Structure deposition date
2017-04-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
9
% buried
96
Peptide accession
Q14204
Residue number A
3712
Residue number B
3808
Peptide name
Cytoplasmic dynein 1 heavy chain 1

Ligandability

Cysteine 3712 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 3808 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Cytoplasmic dynein 1 heavy chain 1 between cysteines 1949 and 1999. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
5nug
Structure name
motor domains from human cytoplasmic dynein-1 in the phi-particle conformation
Structure deposition date
2017-04-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
66
Peptide accession
Q14204
Residue number A
1949
Residue number B
1999
Peptide name
Cytoplasmic dynein 1 heavy chain 1

Ligandability

Cysteine 1949 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1999 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Cytoplasmic dynein 1 heavy chain 1 between cysteines 4510 and 4644. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
8dyu
Structure name
structure of human cytoplasmic dynein-1 bound to two lis1 proteins
Structure deposition date
2022-08-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
51
Peptide accession
Q14204
Residue number A
4510
Residue number B
4644
Peptide name
Cytoplasmic dynein 1 heavy chain 1

Ligandability

Cysteine 4510 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4644 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Cytoplasmic dynein 1 heavy chain 1 between cysteines 3323 and 3387. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
3wuq
Structure name
structure of the entire stalk region of the dynein motor domain
Structure deposition date
2014-05-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
68
Peptide accession
Q9JHU4
Residue number A
3323
Residue number B
3387
Peptide name
Cytoplasmic dynein 1 heavy chain 1

Ligandability

Cysteine 3323 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 3387 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Cytoplasmic dynein 1 heavy chain 1 between cysteines 1949 and 1977. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
5nug
Structure name
motor domains from human cytoplasmic dynein-1 in the phi-particle conformation
Structure deposition date
2017-04-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
89
Peptide accession
Q14204
Residue number A
1949
Residue number B
1977
Peptide name
Cytoplasmic dynein 1 heavy chain 1

Ligandability

Cysteine 1949 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1977 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Cytoplasmic dynein 1 heavy chain 1 between cysteines 2663 and 2712. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
8dyv
Structure name
structure of human cytoplasmic dynein-1 bound to one lis1
Structure deposition date
2022-08-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
13
% buried
100
Peptide accession
Q14204
Residue number A
2663
Residue number B
2712
Peptide name
Cytoplasmic dynein 1 heavy chain 1

Ligandability

Cysteine 2663 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 2712 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Cytoplasmic dynein 1 heavy chain 1 between cysteines 1888 and 1956. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
5nug
Structure name
motor domains from human cytoplasmic dynein-1 in the phi-particle conformation
Structure deposition date
2017-04-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
100
Peptide accession
Q14204
Residue number A
1888
Residue number B
1956
Peptide name
Cytoplasmic dynein 1 heavy chain 1

Ligandability

Cysteine 1888 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1956 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Cytoplasmic dynein 1 heavy chain 1 between cysteines 1932 and 1956. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
5nug
Structure name
motor domains from human cytoplasmic dynein-1 in the phi-particle conformation
Structure deposition date
2017-04-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
13
% buried
100
Peptide accession
Q14204
Residue number A
1932
Residue number B
1956
Peptide name
Cytoplasmic dynein 1 heavy chain 1

Ligandability

Cysteine 1932 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1956 of Cytoplasmic dynein 1 heavy chain 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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