ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Replication protein A 70 kDa DNA-binding subunit

Intramolecular
Cysteine 486 and cysteine 500 L
Cysteine 481 and cysteine 503 L
Cysteine 481 and cysteine 486 L
Cysteine 500 and cysteine 503
Cysteine 481 and cysteine 500 L
Cysteine 200 and cysteine 289
Cysteine 486 and cysteine 503 L
Cysteine 75 and cysteine 77
A redox-regulated disulphide may form within Replication protein A 70 kDa DNA-binding subunit between cysteines 486 and 500.

Details

Redox score ?
91
PDB code
1l1o
Structure name
structure of the human replication protein a (rpa) trimerization core
Structure deposition date
2002-02-19
Thiol separation (Å)
3
Half-sphere exposure sum ?
46
Minimum pKa ?
6
% buried
0
Peptide accession
P27694
Residue number A
486
Residue number B
500
Peptide name
Replication protein A 70 kDa DNA-binding subunit

Ligandability

Cysteine 486 of Replication protein A 70 kDa DNA-binding subunit

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 500 of Replication protein A 70 kDa DNA-binding subunit

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 protein A 70 kDa DNA-binding subunit between cysteines 481 and 503.

Details

Redox score ?
87
PDB code
1l1o
Structure name
structure of the human replication protein a (rpa) trimerization core
Structure deposition date
2002-02-19
Thiol separation (Å)
3
Half-sphere exposure sum ?
51
Minimum pKa ?
7
% buried
0
Peptide accession
P27694
Residue number A
481
Residue number B
503
Peptide name
Replication protein A 70 kDa DNA-binding subunit

Ligandability

Cysteine 481 of Replication protein A 70 kDa DNA-binding subunit

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 503 of Replication protein A 70 kDa DNA-binding subunit

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 protein A 70 kDa DNA-binding subunit between cysteines 481 and 486.

Details

Redox score ?
87
PDB code
1l1o
Structure name
structure of the human replication protein a (rpa) trimerization core
Structure deposition date
2002-02-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
1
Peptide accession
P27694
Residue number A
481
Residue number B
486
Peptide name
Replication protein A 70 kDa DNA-binding subunit

Ligandability

Cysteine 481 of Replication protein A 70 kDa DNA-binding subunit

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 486 of Replication protein A 70 kDa DNA-binding subunit

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 protein A 70 kDa DNA-binding subunit between cysteines 500 and 503.

Details

Redox score ?
87
PDB code
1l1o
Structure name
structure of the human replication protein a (rpa) trimerization core
Structure deposition date
2002-02-19
Thiol separation (Å)
3
Half-sphere exposure sum ?
46
Minimum pKa ?
7
% buried
0
Peptide accession
P27694
Residue number A
500
Residue number B
503
Peptide name
Replication protein A 70 kDa DNA-binding subunit

Ligandability

Cysteine 500 of Replication protein A 70 kDa DNA-binding subunit

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 503 of Replication protein A 70 kDa DNA-binding subunit

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 protein A 70 kDa DNA-binding subunit between cysteines 481 and 500.

Details

Redox score ?
82
PDB code
1l1o
Structure name
structure of the human replication protein a (rpa) trimerization core
Structure deposition date
2002-02-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
1
Peptide accession
P27694
Residue number A
481
Residue number B
500
Peptide name
Replication protein A 70 kDa DNA-binding subunit

Ligandability

Cysteine 481 of Replication protein A 70 kDa DNA-binding subunit

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 500 of Replication protein A 70 kDa DNA-binding subunit

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 protein A 70 kDa DNA-binding subunit between cysteines 200 and 289.

Details

Redox score ?
81
PDB code
1fgu
Structure name
ssdna-binding domain of the large subunit of replication protein a
Structure deposition date
2000-07-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
14
Peptide accession
P27694
Residue number A
200
Residue number B
289
Peptide name
Replication protein A 70 kDa DNA-binding subunit

Ligandability

Cysteine 200 of Replication protein A 70 kDa DNA-binding subunit

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 289 of Replication protein A 70 kDa DNA-binding subunit

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 protein A 70 kDa DNA-binding subunit between cysteines 486 and 503.

Details

Redox score ?
80
PDB code
1l1o
Structure name
structure of the human replication protein a (rpa) trimerization core
Structure deposition date
2002-02-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
9
% buried
0
Peptide accession
P27694
Residue number A
486
Residue number B
503
Peptide name
Replication protein A 70 kDa DNA-binding subunit

Ligandability

Cysteine 486 of Replication protein A 70 kDa DNA-binding subunit

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 503 of Replication protein A 70 kDa DNA-binding subunit

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 protein A 70 kDa DNA-binding subunit between cysteines 75 and 77.

Details

Redox score ?
72
PDB code
4r4c
Structure name
structure of rpa70n in complex with 5-(4-((4-(5-carboxyfuran-2-yl)-2- chlorobenzamido)methyl)phenyl)-1-(3,4-dichlorophenyl)-1h-pyrazole-3- carboxylic acid
Structure deposition date
2014-08-19
Thiol separation (Å)
3
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
71
Peptide accession
P27694
Residue number A
75
Residue number B
77
Peptide name
Replication protein A 70 kDa DNA-binding subunit

Ligandability

Cysteine 75 of Replication protein A 70 kDa DNA-binding subunit

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 77 of Replication protein A 70 kDa DNA-binding subunit

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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