ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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DNA dC->dU-editing enzyme APOBEC-3F

Intramolecular
Cysteine 280 and cysteine 283
Cysteine 248 and cysteine 253
Cysteine 219 and cysteine 339
Cysteine 253 and cysteine 283
Cysteine 248 and cysteine 283
A redox-regulated disulphide may form within DNA dC->dU-editing enzyme APOBEC-3F between cysteines 280 and 283.

Details

Redox score ?
84
PDB code
4j4j
Structure name
crystal structure of the apobec3f vif binding domain
Structure deposition date
2013-02-06
Thiol separation (Å)
3
Half-sphere exposure sum ?
70
Minimum pKa ?
5
% buried
50
Peptide accession
Q8IUX4
Residue number A
280
Residue number B
283
Peptide name
DNA dC->dU-editing enzyme APOBEC-3F

Ligandability

Cysteine 280 of DNA dC->dU-editing enzyme APOBEC-3F

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 283 of DNA dC->dU-editing enzyme APOBEC-3F

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 DNA dC->dU-editing enzyme APOBEC-3F between cysteines 248 and 253.

Details

Redox score ?
73
PDB code
4j4j
Structure name
crystal structure of the apobec3f vif binding domain
Structure deposition date
2013-02-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
16
Peptide accession
Q8IUX4
Residue number A
248
Residue number B
253
Peptide name
DNA dC->dU-editing enzyme APOBEC-3F

Ligandability

Cysteine 248 of DNA dC->dU-editing enzyme APOBEC-3F

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 253 of DNA dC->dU-editing enzyme APOBEC-3F

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 DNA dC->dU-editing enzyme APOBEC-3F between cysteines 219 and 339.

Details

Redox score ?
62
PDB code
5hx4
Structure name
zinc-free apobec3f catalytic domain crystal structure
Structure deposition date
2016-01-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
92
Minimum pKa ?
9
% buried
100
Peptide accession
Q8IUX4
Residue number A
219
Residue number B
339
Peptide name
DNA dC->dU-editing enzyme APOBEC-3F

Ligandability

Cysteine 219 of DNA dC->dU-editing enzyme APOBEC-3F

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 339 of DNA dC->dU-editing enzyme APOBEC-3F

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 DNA dC->dU-editing enzyme APOBEC-3F between cysteines 253 and 283. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
5w2m
Structure name
apobec3f catalytic domain complex with a single-stranded dna
Structure deposition date
2017-06-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
nan
Peptide accession
Q8IUX4
Residue number A
253
Residue number B
283
Peptide name
DNA dC->dU-editing enzyme APOBEC-3F

Ligandability

Cysteine 253 of DNA dC->dU-editing enzyme APOBEC-3F

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 283 of DNA dC->dU-editing enzyme APOBEC-3F

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 DNA dC->dU-editing enzyme APOBEC-3F between cysteines 248 and 283. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
5w2m
Structure name
apobec3f catalytic domain complex with a single-stranded dna
Structure deposition date
2017-06-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
nan
Peptide accession
Q8IUX4
Residue number A
248
Residue number B
283
Peptide name
DNA dC->dU-editing enzyme APOBEC-3F

Ligandability

Cysteine 248 of DNA dC->dU-editing enzyme APOBEC-3F

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 283 of DNA dC->dU-editing enzyme APOBEC-3F

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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