ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Coatomer subunit gamma-1

Intramolecular
Cysteine 665 and cysteine 706
Cysteine 650 and cysteine 726 L
Cysteine 650 and cysteine 665
Cysteine 97 and cysteine 169
Cysteine 722 and cysteine 726 L
Cysteine 44 and cysteine 88
Cysteine 129 and cysteine 169
Cysteine 650 and cysteine 706
A redox-regulated disulphide may form within Coatomer subunit gamma-1 between cysteines 665 and 706.

Details

Redox score ?
69
PDB code
1pzd
Structure name
structural identification of a conserved appendage domain in the carboxyl-terminus of the copi gamma-subunit
Structure deposition date
2003-07-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
9
% buried
97
Peptide accession
P53620
Residue number A
665
Residue number B
706
Peptide name
Coatomer subunit gamma-1

Ligandability

Cysteine 665 of Coatomer subunit gamma-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 706 of Coatomer subunit gamma-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 Coatomer subunit gamma-1 between cysteines 650 and 726. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
1r4x
Structure name
crystal structure analys of the gamma-copi appendage domain
Structure deposition date
2003-10-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
12
% buried
87
Peptide accession
Q9Y678
Residue number A
650
Residue number B
726
Peptide name
Coatomer subunit gamma-1

Ligandability

Cysteine 650 of Coatomer subunit gamma-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 726 of Coatomer subunit gamma-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 Coatomer subunit gamma-1 between cysteines 650 and 665. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
1r4x
Structure name
crystal structure analys of the gamma-copi appendage domain
Structure deposition date
2003-10-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
9
% buried
95
Peptide accession
Q9Y678
Residue number A
650
Residue number B
665
Peptide name
Coatomer subunit gamma-1

Ligandability

Cysteine 650 of Coatomer subunit gamma-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 665 of Coatomer subunit gamma-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 Coatomer subunit gamma-1 between cysteines 97 and 169. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
3tjz
Structure name
crystal structure of arf1 bound to the gamma/zeta-cop core complex
Structure deposition date
2011-08-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
21
Peptide accession
P53620
Residue number A
97
Residue number B
169
Peptide name
Coatomer subunit gamma-1

Ligandability

Cysteine 97 of Coatomer subunit gamma-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 169 of Coatomer subunit gamma-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 Coatomer subunit gamma-1 between cysteines 722 and 726. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
1r4x
Structure name
crystal structure analys of the gamma-copi appendage domain
Structure deposition date
2003-10-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
60
Peptide accession
Q9Y678
Residue number A
722
Residue number B
726
Peptide name
Coatomer subunit gamma-1

Ligandability

Cysteine 722 of Coatomer subunit gamma-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 726 of Coatomer subunit gamma-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 Coatomer subunit gamma-1 between cysteines 44 and 88. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3tjz
Structure name
crystal structure of arf1 bound to the gamma/zeta-cop core complex
Structure deposition date
2011-08-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
11
% buried
72
Peptide accession
P53620
Residue number A
44
Residue number B
88
Peptide name
Coatomer subunit gamma-1

Ligandability

Cysteine 44 of Coatomer subunit gamma-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 88 of Coatomer subunit gamma-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 Coatomer subunit gamma-1 between cysteines 129 and 169. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3tjz
Structure name
crystal structure of arf1 bound to the gamma/zeta-cop core complex
Structure deposition date
2011-08-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
78
Peptide accession
P53620
Residue number A
129
Residue number B
169
Peptide name
Coatomer subunit gamma-1

Ligandability

Cysteine 129 of Coatomer subunit gamma-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 169 of Coatomer subunit gamma-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 Coatomer subunit gamma-1 between cysteines 650 and 706. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
1pzd
Structure name
structural identification of a conserved appendage domain in the carboxyl-terminus of the copi gamma-subunit
Structure deposition date
2003-07-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
13
% buried
100
Peptide accession
P53620
Residue number A
650
Residue number B
706
Peptide name
Coatomer subunit gamma-1

Ligandability

Cysteine 650 of Coatomer subunit gamma-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 706 of Coatomer subunit gamma-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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