ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Clathrin heavy chain

Intramolecular
Cysteine 1257 and cysteine 1260
Cysteine 1565 and cysteine 1569
Cysteine 1260 and cysteine 1272
Cysteine 918 and cysteine 934
Cysteine 1257 and cysteine 1272
Cysteine 1569 and cysteine 1573
Cysteine 666 and cysteine 682
A redox-regulated disulphide may form within Clathrin heavy chain between cysteines 1257 and 1260.

Details

Redox score ?
61
PDB code
6sct
Structure name
cryo-em structure of the consensus triskelion hub of the clathrin coat complex
Structure deposition date
2019-07-25
Thiol separation (Å)
6
Half-sphere exposure sum ?
76
Minimum pKa ?
8
% buried
77
Peptide accession
C0MHR2
Residue number A
1257
Residue number B
1260
Peptide name
Clathrin heavy chain

Ligandability

Cysteine 1257 of Clathrin heavy chain

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 1260 of Clathrin heavy chain

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 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 ?
59
PDB code
6sct
Structure name
cryo-em structure of the consensus triskelion hub of the clathrin coat complex
Structure deposition date
2019-07-25
Thiol separation (Å)
5
Half-sphere exposure sum ?
78
Minimum pKa ?
10
% buried
81
Peptide accession
C0MHR2
Residue number A
1565
Residue number B
1569
Peptide name
Clathrin heavy chain

Ligandability

Cysteine 1565 of Clathrin heavy chain

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 1569 of Clathrin heavy chain

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

Details

Redox score ?
59
PDB code
6sct
Structure name
cryo-em structure of the consensus triskelion hub of the clathrin coat complex
Structure deposition date
2019-07-25
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
74
Peptide accession
C0MHR2
Residue number A
1260
Residue number B
1272
Peptide name
Clathrin heavy chain

Ligandability

Cysteine 1260 of Clathrin heavy chain

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 1272 of Clathrin heavy chain

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 between cysteines 918 and 934. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
6sct
Structure name
cryo-em structure of the consensus triskelion hub of the clathrin coat complex
Structure deposition date
2019-07-25
Thiol separation (Å)
5
Half-sphere exposure sum ?
84
Minimum pKa ?
11
% buried
84
Peptide accession
C0MHR2
Residue number A
918
Residue number B
934
Peptide name
Clathrin heavy chain

Ligandability

Cysteine 918 of Clathrin heavy chain

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

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

Details

Redox score ?
54
PDB code
6sct
Structure name
cryo-em structure of the consensus triskelion hub of the clathrin coat complex
Structure deposition date
2019-07-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
36
Peptide accession
C0MHR2
Residue number A
1257
Residue number B
1272
Peptide name
Clathrin heavy chain

Ligandability

Cysteine 1257 of Clathrin heavy chain

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 1272 of Clathrin heavy chain

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 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 ?
45
PDB code
6sct
Structure name
cryo-em structure of the consensus triskelion hub of the clathrin coat complex
Structure deposition date
2019-07-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
98
Peptide accession
C0MHR2
Residue number A
1569
Residue number B
1573
Peptide name
Clathrin heavy chain

Ligandability

Cysteine 1569 of Clathrin heavy chain

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 1573 of Clathrin heavy chain

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 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 ?
40
PDB code
6sct
Structure name
cryo-em structure of the consensus triskelion hub of the clathrin coat complex
Structure deposition date
2019-07-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
64
Peptide accession
C0MHR2
Residue number A
666
Residue number B
682
Peptide name
Clathrin heavy chain

Ligandability

Cysteine 666 of Clathrin heavy chain

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

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.

If this tool was useful for finding a disulphide, please cite: