ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

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

Intramolecular
Cysteine 97 and cysteine 100
Cysteine 280 and cysteine 283
Cysteine 288 and cysteine 321
Cysteine 221 and cysteine 346
Cysteine 261 and cysteine 281
Cysteine 36 and cysteine 160
Cysteine 346 and cysteine 356
Cysteine 261 and cysteine 288
Cysteine 243 and cysteine 261
Cysteine 261 and cysteine 291
More...
Cysteine 221 and cysteine 243
Cysteine 291 and cysteine 321
Cysteine 281 and cysteine 308
Cysteine 29 and cysteine 30
Cysteine 308 and cysteine 346
Cysteine 221 and cysteine 281
Cysteine 281 and cysteine 291
Cysteine 281 and cysteine 346
Cysteine 221 and cysteine 261
A redox-regulated disulphide may form within DNA dC->dU-editing enzyme APOBEC-3G between cysteines 97 and 100.

Details

Redox score ?
93
PDB code
8cx1
Structure name
cryo-em structure of human apobec3g/hiv-1 vif/cbfbeta/elob/eloc dimeric complex in state 1
Structure deposition date
2022-05-19
Thiol separation (Å)
3
Half-sphere exposure sum ?
66
Minimum pKa ?
0
% buried
100
Peptide accession
Q9HC16
Residue number A
97
Residue number B
100
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

Cysteine 97 of DNA dC->dU-editing enzyme APOBEC-3G

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 100 of DNA dC->dU-editing enzyme APOBEC-3G

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-3G between cysteines 280 and 283 (287 and 290 respectively in this structure).

Details

Redox score ?
82
PDB code
8e40
Structure name
full-length apobec3g in complex with hiv-1 vif, cbf-beta, and fork rna
Structure deposition date
2022-08-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
60
Minimum pKa ?
5
% buried
62
Peptide accession
Q7YR23
Residue number A
280
Residue number B
283
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

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

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-3G

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-3G between cysteines 288 and 321.

Details

Redox score ?
71
PDB code
3iqs
Structure name
crystal structure of the anti-viral apobec3g catalytic domain
Structure deposition date
2009-08-20
Thiol separation (Å)
6
Half-sphere exposure sum ?
58
Minimum pKa ?
4
% buried
40
Peptide accession
Q9HC16
Residue number A
288
Residue number B
321
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

Cysteine 288 of DNA dC->dU-editing enzyme APOBEC-3G

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 321 of DNA dC->dU-editing enzyme APOBEC-3G

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-3G between cysteines 221 and 346.

Details

Redox score ?
61
PDB code
3e1u
Structure name
the crystal structure of the anti-viral apobec3g catalytic domain
Structure deposition date
2008-08-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
80
Minimum pKa ?
9
% buried
97
Peptide accession
Q9HC16
Residue number A
221
Residue number B
346
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

Cysteine 221 of DNA dC->dU-editing enzyme APOBEC-3G

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 346 of DNA dC->dU-editing enzyme APOBEC-3G

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-3G between cysteines 261 and 281 (71 and 91 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
2kbo
Structure name
structure, interaction, and real-time monitoring of the enzymatic reaction of wild type apobec3g
Structure deposition date
2008-12-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
86
Peptide accession
Q9HC16
Residue number A
261
Residue number B
281
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

Cysteine 261 of DNA dC->dU-editing enzyme APOBEC-3G

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 281 of DNA dC->dU-editing enzyme APOBEC-3G

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-3G between cysteines 36 and 160. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
8cx2
Structure name
cryo-em structure of human apobec3g/hiv-1 vif/cbfbeta/elob/eloc dimeric complex in state 2
Structure deposition date
2022-05-19
Thiol separation (Å)
5
Half-sphere exposure sum ?
81
Minimum pKa ?
13
% buried
100
Peptide accession
Q9HC16
Residue number A
36
Residue number B
160
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

Cysteine 36 of DNA dC->dU-editing enzyme APOBEC-3G

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 160 of DNA dC->dU-editing enzyme APOBEC-3G

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-3G between cysteines 346 and 356 (156 and 166 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
2kbo
Structure name
structure, interaction, and real-time monitoring of the enzymatic reaction of wild type apobec3g
Structure deposition date
2008-12-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
40
Peptide accession
Q9HC16
Residue number A
346
Residue number B
356
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

Cysteine 346 of DNA dC->dU-editing enzyme APOBEC-3G

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 356 of DNA dC->dU-editing enzyme APOBEC-3G

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-3G between cysteines 261 and 288. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
6k3k
Structure name
solution structure of apobec3g-cd2 with ssdna, product b
Structure deposition date
2019-05-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
4
% buried
64
Peptide accession
Q9HC16
Residue number A
261
Residue number B
288
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

Cysteine 261 of DNA dC->dU-editing enzyme APOBEC-3G

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 288 of DNA dC->dU-editing enzyme APOBEC-3G

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-3G between cysteines 243 and 261. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
4row
Structure name
the crystal structure of novel apobec3g cd2 head-to-tail dimer suggests the binding mode of full-length apobec3g to hiv-1 ssdna
Structure deposition date
2014-10-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
48
Peptide accession
Q9HC16
Residue number A
243
Residue number B
261
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

Cysteine 243 of DNA dC->dU-editing enzyme APOBEC-3G

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 261 of DNA dC->dU-editing enzyme APOBEC-3G

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-3G between cysteines 261 and 291. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
3iqs
Structure name
crystal structure of the anti-viral apobec3g catalytic domain
Structure deposition date
2009-08-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
11
% buried
49
Peptide accession
Q9HC16
Residue number A
261
Residue number B
291
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

Cysteine 261 of DNA dC->dU-editing enzyme APOBEC-3G

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 291 of DNA dC->dU-editing enzyme APOBEC-3G

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-3G between cysteines 221 and 243 (31 and 53 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2kbo
Structure name
structure, interaction, and real-time monitoring of the enzymatic reaction of wild type apobec3g
Structure deposition date
2008-12-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
44
Peptide accession
Q9HC16
Residue number A
221
Residue number B
243
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

Cysteine 221 of DNA dC->dU-editing enzyme APOBEC-3G

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 243 of DNA dC->dU-editing enzyme APOBEC-3G

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-3G between cysteines 291 and 321. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3iqs
Structure name
crystal structure of the anti-viral apobec3g catalytic domain
Structure deposition date
2009-08-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
11
% buried
50
Peptide accession
Q9HC16
Residue number A
291
Residue number B
321
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

Cysteine 291 of DNA dC->dU-editing enzyme APOBEC-3G

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 321 of DNA dC->dU-editing enzyme APOBEC-3G

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-3G between cysteines 281 and 308. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
4rov
Structure name
the crystal structure of novel apobec3g cd2 head-to-tail dimer suggests the binding mode of full-length apobec3g to hiv-1 ssdna
Structure deposition date
2014-10-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
78
Peptide accession
Q9HC16
Residue number A
281
Residue number B
308
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

Cysteine 281 of DNA dC->dU-editing enzyme APOBEC-3G

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 308 of DNA dC->dU-editing enzyme APOBEC-3G

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-3G between cysteines 29 and 30 (36 and 37 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
8e40
Structure name
full-length apobec3g in complex with hiv-1 vif, cbf-beta, and fork rna
Structure deposition date
2022-08-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
100
Peptide accession
Q7YR23
Residue number A
29
Residue number B
30
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

Cysteine 29 of DNA dC->dU-editing enzyme APOBEC-3G

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 30 of DNA dC->dU-editing enzyme APOBEC-3G

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-3G between cysteines 308 and 346. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6k3j
Structure name
solution structure of apobec3g-cd2 with ssdna, product a
Structure deposition date
2019-05-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
58
Peptide accession
Q9HC16
Residue number A
308
Residue number B
346
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

Cysteine 308 of DNA dC->dU-editing enzyme APOBEC-3G

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 346 of DNA dC->dU-editing enzyme APOBEC-3G

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-3G between cysteines 221 and 281. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3ir2
Structure name
crystal structure of the apobec3g catalytic domain
Structure deposition date
2009-08-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
9
% buried
100
Peptide accession
Q9HC16
Residue number A
221
Residue number B
281
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

Cysteine 221 of DNA dC->dU-editing enzyme APOBEC-3G

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 281 of DNA dC->dU-editing enzyme APOBEC-3G

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-3G between cysteines 281 and 291 (91 and 101 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
2kbo
Structure name
structure, interaction, and real-time monitoring of the enzymatic reaction of wild type apobec3g
Structure deposition date
2008-12-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
86
Peptide accession
Q9HC16
Residue number A
281
Residue number B
291
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

Cysteine 281 of DNA dC->dU-editing enzyme APOBEC-3G

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 291 of DNA dC->dU-editing enzyme APOBEC-3G

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-3G between cysteines 281 and 346. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
4row
Structure name
the crystal structure of novel apobec3g cd2 head-to-tail dimer suggests the binding mode of full-length apobec3g to hiv-1 ssdna
Structure deposition date
2014-10-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
13
% buried
100
Peptide accession
Q9HC16
Residue number A
281
Residue number B
346
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

Cysteine 281 of DNA dC->dU-editing enzyme APOBEC-3G

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 346 of DNA dC->dU-editing enzyme APOBEC-3G

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-3G between cysteines 221 and 261 (24 and 64 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
2jyw
Structure name
solution structure of c-terminal domain of apobec3g
Structure deposition date
2007-12-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
92
Peptide accession
Q9HC16
Residue number A
221
Residue number B
261
Peptide name
DNA dC->dU-editing enzyme APOBEC-3G

Ligandability

Cysteine 221 of DNA dC->dU-editing enzyme APOBEC-3G

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 261 of DNA dC->dU-editing enzyme APOBEC-3G

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: