ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Clathrin heavy chain 1

Intermolecular
Cysteine 1569 and cysteine 198 of Clathrin light chain B L
Cysteine 1573 and cysteine 198 of Clathrin light chain B L
Cysteine 1565 and cysteine 198 of Clathrin light chain B L
Intramolecular
Cysteine 918 and cysteine 934 L
Cysteine 1260 and cysteine 1272 L
Cysteine 1257 and cysteine 1272 L
Cysteine 1257 and cysteine 1260 L
Cysteine 1565 and cysteine 1569 L
Cysteine 1569 and cysteine 1573 L
Cysteine 436 and cysteine 459
More...
Cysteine 666 and cysteine 682
Cysteine 748 and cysteine 778 L
Cysteine 736 and cysteine 748
Cysteine 909 and cysteine 918
A redox-regulated disulphide may form between cysteine 1569 of Clathrin heavy chain 1 and cysteine 198 of Clathrin light chain B. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
6wcj
Structure name
asymmetric vertex of the clathrin minicoat cage
Structure deposition date
2020-03-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
88
Peptide A name
Clathrin heavy chain 1
Peptide B name
Clathrin light chain B
Peptide A accession
P49951
Peptide B accession
P04975
Peptide A residue number
1569
Peptide B residue number
198

Ligandability

Cysteine 1569 of Clathrin 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 198 of Clathrin light chain B

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.

A redox-regulated disulphide may form between cysteine 1573 of Clathrin heavy chain 1 and cysteine 198 of Clathrin light chain B. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6wcj
Structure name
asymmetric vertex of the clathrin minicoat cage
Structure deposition date
2020-03-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
85
Peptide A name
Clathrin heavy chain 1
Peptide B name
Clathrin light chain B
Peptide A accession
P49951
Peptide B accession
P04975
Peptide A residue number
1573
Peptide B residue number
198

Ligandability

Cysteine 1573 of Clathrin 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 198 of Clathrin light chain B

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.

A redox-regulated disulphide may form between cysteine 1565 of Clathrin heavy chain 1 and cysteine 198 of Clathrin light chain B. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6wcj
Structure name
asymmetric vertex of the clathrin minicoat cage
Structure deposition date
2020-03-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
76
Peptide A name
Clathrin heavy chain 1
Peptide B name
Clathrin light chain B
Peptide A accession
P49951
Peptide B accession
P04975
Peptide A residue number
1565
Peptide B residue number
198

Ligandability

Cysteine 1565 of Clathrin 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 198 of Clathrin light chain B

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.

A redox-regulated disulphide may form within Clathrin heavy chain 1 between cysteines 918 and 934.

Details

Redox score ?
74
PDB code
6wcj
Structure name
asymmetric vertex of the clathrin minicoat cage
Structure deposition date
2020-03-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
7
% buried
85
Peptide accession
P49951
Residue number A
918
Residue number B
934
Peptide name
Clathrin heavy chain 1

Ligandability

Cysteine 918 of Clathrin 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 934 of Clathrin 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Clathrin heavy chain 1 between cysteines 1260 and 1272.

Details

Redox score ?
67
PDB code
1b89
Structure name
clathrin heavy chain proximal leg segment (bovine)
Structure deposition date
1999-05-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
11
% buried
65
Peptide accession
P49951
Residue number A
1260
Residue number B
1272
Peptide name
Clathrin heavy chain 1

Ligandability

Cysteine 1260 of Clathrin 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 1272 of Clathrin 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 Clathrin heavy chain 1 between cysteines 1257 and 1272.

Details

Redox score ?
61
PDB code
1b89
Structure name
clathrin heavy chain proximal leg segment (bovine)
Structure deposition date
1999-05-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
12
% buried
86
Peptide accession
P49951
Residue number A
1257
Residue number B
1272
Peptide name
Clathrin heavy chain 1

Ligandability

Cysteine 1257 of Clathrin 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 1272 of Clathrin 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 Clathrin heavy chain 1 between cysteines 1257 and 1260. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
60
PDB code
3lvh
Structure name
crystal structure of a clathrin heavy chain and clathrin light chain complex
Structure deposition date
2010-02-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
77
Peptide accession
P49951
Residue number A
1257
Residue number B
1260
Peptide name
Clathrin heavy chain 1

Ligandability

Cysteine 1257 of Clathrin 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 1260 of Clathrin 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Clathrin heavy chain 1 between cysteines 1565 and 1569. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
3qil
Structure name
crystal structure analysis of the clathrin trimerization domain
Structure deposition date
2011-01-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
53
Peptide accession
P49951
Residue number A
1565
Residue number B
1569
Peptide name
Clathrin heavy chain 1

Ligandability

Cysteine 1565 of Clathrin 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 1569 of Clathrin 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Clathrin heavy chain 1 between cysteines 1569 and 1573. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3qil
Structure name
crystal structure analysis of the clathrin trimerization domain
Structure deposition date
2011-01-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
60
Peptide accession
P49951
Residue number A
1569
Residue number B
1573
Peptide name
Clathrin heavy chain 1

Ligandability

Cysteine 1569 of Clathrin 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 1573 of Clathrin 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Clathrin heavy chain 1 between cysteines 436 and 459. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
1bpo
Structure name
clathrin heavy-chain terminal domain and linker
Structure deposition date
1998-08-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
91
Peptide accession
P11442
Residue number A
436
Residue number B
459
Peptide name
Clathrin heavy chain 1

Ligandability

Cysteine 436 of Clathrin 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 459 of Clathrin 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 Clathrin heavy chain 1 between cysteines 666 and 682. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6wcj
Structure name
asymmetric vertex of the clathrin minicoat cage
Structure deposition date
2020-03-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
64
Peptide accession
P49951
Residue number A
666
Residue number B
682
Peptide name
Clathrin heavy chain 1

Ligandability

Cysteine 666 of Clathrin 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 682 of Clathrin 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 Clathrin heavy chain 1 between cysteines 748 and 778. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6wcj
Structure name
asymmetric vertex of the clathrin minicoat cage
Structure deposition date
2020-03-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
79
Peptide accession
P49951
Residue number A
748
Residue number B
778
Peptide name
Clathrin heavy chain 1

Ligandability

Cysteine 748 of Clathrin 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 778 of Clathrin 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Clathrin heavy chain 1 between cysteines 736 and 748. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6wcj
Structure name
asymmetric vertex of the clathrin minicoat cage
Structure deposition date
2020-03-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
72
Peptide accession
P49951
Residue number A
736
Residue number B
748
Peptide name
Clathrin heavy chain 1

Ligandability

Cysteine 736 of Clathrin 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 748 of Clathrin 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 Clathrin heavy chain 1 between cysteines 909 and 918. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
6wcj
Structure name
asymmetric vertex of the clathrin minicoat cage
Structure deposition date
2020-03-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
83
Peptide accession
P49951
Residue number A
909
Residue number B
918
Peptide name
Clathrin heavy chain 1

Ligandability

Cysteine 909 of Clathrin 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 918 of Clathrin 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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