ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Replication factor C subunit 2

Intramolecular
Cysteine 270 and cysteine 345
Cysteine 270 and cysteine 303
Cysteine 171 and cysteine 185
A redox-regulated disulphide may form within Replication factor C subunit 2 between cysteines 270 and 345.

Details

Redox score ?
72
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)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
86
Peptide accession
P35250
Residue number A
270
Residue number B
345
Peptide name
Replication factor C subunit 2

Ligandability

Cysteine 270 of Replication factor C subunit 2

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 345 of Replication factor C subunit 2

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 2 between cysteines 270 and 303. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
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 ?
75
Minimum pKa ?
12
% buried
97
Peptide accession
P35250
Residue number A
270
Residue number B
303
Peptide name
Replication factor C subunit 2

Ligandability

Cysteine 270 of Replication factor C subunit 2

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 303 of Replication factor C subunit 2

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 2 between cysteines 171 and 185. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
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 ?
80
Minimum pKa ?
13
% buried
98
Peptide accession
P35250
Residue number A
171
Residue number B
185
Peptide name
Replication factor C subunit 2

Ligandability

Cysteine 171 of Replication factor C subunit 2

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 185 of Replication factor C subunit 2

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: