ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Replication factor C subunit 5

Intramolecular
Cysteine 73 and cysteine 152 L
Cysteine 155 and cysteine 169
Cysteine 152 and cysteine 169 L
Cysteine 152 and cysteine 155 L
A redox-regulated disulphide may form within Replication factor C subunit 5 between cysteines 73 and 152. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
6vvo
Structure name
structure of the human clamp loader (replication factor c, rfc) bound to the sliding clamp (proliferating cell nuclear antigen, pcna)
Structure deposition date
2020-02-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
94
Peptide accession
P40937
Residue number A
73
Residue number B
152
Peptide name
Replication factor C subunit 5

Ligandability

Cysteine 73 of Replication factor C subunit 5

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 152 of Replication factor C subunit 5

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 Replication factor C subunit 5 between cysteines 155 and 169. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6vvo
Structure name
structure of the human clamp loader (replication factor c, rfc) bound to the sliding clamp (proliferating cell nuclear antigen, pcna)
Structure deposition date
2020-02-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
97
Peptide accession
P40937
Residue number A
155
Residue number B
169
Peptide name
Replication factor C subunit 5

Ligandability

Cysteine 155 of Replication factor C subunit 5

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 Replication factor C subunit 5

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 Replication factor C subunit 5 between cysteines 152 and 169. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
6vvo
Structure name
structure of the human clamp loader (replication factor c, rfc) bound to the sliding clamp (proliferating cell nuclear antigen, pcna)
Structure deposition date
2020-02-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
100
Peptide accession
P40937
Residue number A
152
Residue number B
169
Peptide name
Replication factor C subunit 5

Ligandability

Cysteine 152 of Replication factor C subunit 5

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 169 of Replication factor C subunit 5

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 Replication factor C subunit 5 between cysteines 152 and 155. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
6vvo
Structure name
structure of the human clamp loader (replication factor c, rfc) bound to the sliding clamp (proliferating cell nuclear antigen, pcna)
Structure deposition date
2020-02-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
97
Peptide accession
P40937
Residue number A
152
Residue number B
155
Peptide name
Replication factor C subunit 5

Ligandability

Cysteine 152 of Replication factor C subunit 5

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 155 of Replication factor C subunit 5

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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