ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Ribonucleoprotein PTB-binding 1

Intramolecular
Cysteine 239 and cysteine 251 L
Cysteine 224 and cysteine 297
Cysteine 222 and cysteine 297
Cysteine 222 and cysteine 224
Cysteine 135 and cysteine 297
A redox-regulated disulphide may form within Ribonucleoprotein PTB-binding 1 between cysteines 239 and 251.

Details

Redox score ?
85
PDB code
3h2u
Structure name
human raver1 rrm1, rrm2, and rrm3 domains in complex with human vinculin tail domain vt
Structure deposition date
2009-04-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8IY67
Residue number A
239
Residue number B
251
Peptide name
Ribonucleoprotein PTB-binding 1

Ligandability

Cysteine 239 of Ribonucleoprotein PTB-binding 1

Cysteine 251 of Ribonucleoprotein PTB-binding 1

A redox-regulated disulphide may form within Ribonucleoprotein PTB-binding 1 between cysteines 224 and 297. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
3vf0
Structure name
raver1 in complex with metavinculin l954 deletion mutant
Structure deposition date
2012-01-09
Thiol separation (Å)
5
Half-sphere exposure sum ?
92
Minimum pKa ?
8
% buried
100
Peptide accession
Q8IY67
Residue number A
224
Residue number B
297
Peptide name
Ribonucleoprotein PTB-binding 1

Ligandability

Cysteine 224 of Ribonucleoprotein PTB-binding 1

Cysteine 297 of Ribonucleoprotein PTB-binding 1

A redox-regulated disulphide may form within Ribonucleoprotein PTB-binding 1 between cysteines 222 and 297. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3vf0
Structure name
raver1 in complex with metavinculin l954 deletion mutant
Structure deposition date
2012-01-09
Thiol separation (Å)
5
Half-sphere exposure sum ?
91
Minimum pKa ?
12
% buried
89
Peptide accession
Q8IY67
Residue number A
222
Residue number B
297
Peptide name
Ribonucleoprotein PTB-binding 1

Ligandability

Cysteine 222 of Ribonucleoprotein PTB-binding 1

Cysteine 297 of Ribonucleoprotein PTB-binding 1

A redox-regulated disulphide may form within Ribonucleoprotein PTB-binding 1 between cysteines 222 and 224. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
3h2u
Structure name
human raver1 rrm1, rrm2, and rrm3 domains in complex with human vinculin tail domain vt
Structure deposition date
2009-04-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
92
Minimum pKa ?
9
% buried
86
Peptide accession
Q8IY67
Residue number A
222
Residue number B
224
Peptide name
Ribonucleoprotein PTB-binding 1

Ligandability

Cysteine 222 of Ribonucleoprotein PTB-binding 1

Cysteine 224 of Ribonucleoprotein PTB-binding 1

A redox-regulated disulphide may form within Ribonucleoprotein PTB-binding 1 between cysteines 135 and 297. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
21
PDB code
3h2u
Structure name
human raver1 rrm1, rrm2, and rrm3 domains in complex with human vinculin tail domain vt
Structure deposition date
2009-04-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
89
Minimum pKa ?
13
% buried
100
Peptide accession
Q8IY67
Residue number A
135
Residue number B
297
Peptide name
Ribonucleoprotein PTB-binding 1

Ligandability

Cysteine 135 of Ribonucleoprotein PTB-binding 1

Cysteine 297 of Ribonucleoprotein PTB-binding 1

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