ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

DNA-binding protein SMUBP-2

Intermolecular
Cysteine 191 and cysteine 191 L
Cysteine 258 and cysteine 191 L
Intramolecular
Cysteine 377 and cysteine 385
Cysteine 377 and cysteine 395
Cysteine 240 and cysteine 241 L
Cysteine 385 and cysteine 395
Cysteine 241 and cysteine 385 L
A redox-regulated disulphide may form between two units of DNA-binding protein SMUBP-2 at cysteines 191 and 191.

Details

Redox score ?
60
PDB code
4b3g
Structure name
crystal structure of ighmbp2 helicase in complex with rna
Structure deposition date
2012-07-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
42
Minimum pKa ?
10
% buried
70
Peptide A name
DNA-binding protein SMUBP-2
Peptide B name
DNA-binding protein SMUBP-2
Peptide A accession
P38935
Peptide B accession
P38935
Peptide A residue number
191
Peptide B residue number
191

Ligandability

A redox-regulated disulphide may form between two units of DNA-binding protein SMUBP-2 at cysteines 258 and 191. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4b3g
Structure name
crystal structure of ighmbp2 helicase in complex with rna
Structure deposition date
2012-07-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
46
Minimum pKa ?
10
% buried
84
Peptide A name
DNA-binding protein SMUBP-2
Peptide B name
DNA-binding protein SMUBP-2
Peptide A accession
P38935
Peptide B accession
P38935
Peptide A residue number
258
Peptide B residue number
191

Ligandability

Cysteine 258 of DNA-binding protein SMUBP-2

Cysteine 191 of DNA-binding protein SMUBP-2

A redox-regulated disulphide may form within DNA-binding protein SMUBP-2 between cysteines 377 and 385.

Details

Redox score ?
69
PDB code
4b3g
Structure name
crystal structure of ighmbp2 helicase in complex with rna
Structure deposition date
2012-07-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
96
Minimum pKa ?
9
% buried
100
Peptide accession
P38935
Residue number A
377
Residue number B
385
Peptide name
DNA-binding protein SMUBP-2

Ligandability

Cysteine 377 of DNA-binding protein SMUBP-2

Cysteine 385 of DNA-binding protein SMUBP-2

A redox-regulated disulphide may form within DNA-binding protein SMUBP-2 between cysteines 377 and 395. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
4b3g
Structure name
crystal structure of ighmbp2 helicase in complex with rna
Structure deposition date
2012-07-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
96
Minimum pKa ?
9
% buried
100
Peptide accession
P38935
Residue number A
377
Residue number B
395
Peptide name
DNA-binding protein SMUBP-2

Ligandability

Cysteine 377 of DNA-binding protein SMUBP-2

Cysteine 395 of DNA-binding protein SMUBP-2

A redox-regulated disulphide may form within DNA-binding protein SMUBP-2 between cysteines 240 and 241. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4b3f
Structure name
crystal structure of ighmbp2 helicase
Structure deposition date
2012-07-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
103
Minimum pKa ?
12
% buried
100
Peptide accession
P38935
Residue number A
240
Residue number B
241
Peptide name
DNA-binding protein SMUBP-2

Ligandability

Cysteine 240 of DNA-binding protein SMUBP-2

Cysteine 241 of DNA-binding protein SMUBP-2

A redox-regulated disulphide may form within DNA-binding protein SMUBP-2 between cysteines 385 and 395. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4b3g
Structure name
crystal structure of ighmbp2 helicase in complex with rna
Structure deposition date
2012-07-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
13
% buried
100
Peptide accession
P38935
Residue number A
385
Residue number B
395
Peptide name
DNA-binding protein SMUBP-2

Ligandability

Cysteine 385 of DNA-binding protein SMUBP-2

Cysteine 395 of DNA-binding protein SMUBP-2

A redox-regulated disulphide may form within DNA-binding protein SMUBP-2 between cysteines 241 and 385. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
4b3f
Structure name
crystal structure of ighmbp2 helicase
Structure deposition date
2012-07-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
12
% buried
100
Peptide accession
P38935
Residue number A
241
Residue number B
385
Peptide name
DNA-binding protein SMUBP-2

Ligandability

Cysteine 241 of DNA-binding protein SMUBP-2

Cysteine 385 of DNA-binding protein SMUBP-2

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