ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Zinc finger protein ZFAT

Intramolecular
Cysteine 939 and cysteine 942
Cysteine 328 and cysteine 331
Cysteine 460 and cysteine 463
Cysteine 911 and cysteine 914
Cysteine 356 and cysteine 359
Cysteine 301 and cysteine 304
Cysteine 772 and cysteine 775
Cysteine 832 and cysteine 835
Cysteine 406 and cysteine 409
Cysteine 273 and cysteine 276
More...
Cysteine 800 and cysteine 805
Cysteine 882 and cysteine 885
Cysteine 328 and cysteine 335
Cysteine 276 and cysteine 304
Cysteine 301 and cysteine 335
Cysteine 331 and cysteine 335
Cysteine 304 and cysteine 335
A redox-regulated disulphide may form within Zinc finger protein ZFAT between cysteines 939 and 942 (12 and 15 respectively in this structure).

Details

Redox score ?
90
PDB code
2rv3
Structure name
solution structures of the dna-binding domain (zf15) of immune-related zinc-finger protein zfat
Structure deposition date
2015-01-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
35
Minimum pKa ?
6
% buried
0
Peptide accession
Q9P243
Residue number A
939
Residue number B
942
Peptide name
Zinc finger protein ZFAT

Ligandability

Cysteine 939 of Zinc finger protein ZFAT

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 942 of Zinc finger protein ZFAT

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 Zinc finger protein ZFAT between cysteines 328 and 331 (67 and 70 respectively in this structure).

Details

Redox score ?
89
PDB code
2rv6
Structure name
solution structures of the dna-binding domains (zf2-zf3-zf4) of immune-related zinc-finger protein zfat
Structure deposition date
2015-01-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
35
Minimum pKa ?
7
% buried
0
Peptide accession
Q9P243
Residue number A
328
Residue number B
331
Peptide name
Zinc finger protein ZFAT

Ligandability

Cysteine 328 of Zinc finger protein ZFAT

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 331 of Zinc finger protein ZFAT

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 Zinc finger protein ZFAT between cysteines 460 and 463 (10 and 13 respectively in this structure).

Details

Redox score ?
89
PDB code
2rv5
Structure name
solution structures of the dna-binding domain (zf8) of mouse immune- related zinc-finger protein zfat
Structure deposition date
2015-01-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
7
% buried
0
Peptide accession
Q7TS63
Residue number A
460
Residue number B
463
Peptide name
Zinc finger protein ZFAT

Ligandability

Cysteine 460 of Zinc finger protein ZFAT

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 463 of Zinc finger protein ZFAT

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 Zinc finger protein ZFAT between cysteines 911 and 914 (12 and 15 respectively in this structure).

Details

Redox score ?
89
PDB code
2rv2
Structure name
solution structures of the dna-binding domain (zf14) of immune-related zinc-finger protein zfat
Structure deposition date
2015-01-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
7
% buried
0
Peptide accession
Q9P243
Residue number A
911
Residue number B
914
Peptide name
Zinc finger protein ZFAT

Ligandability

Cysteine 911 of Zinc finger protein ZFAT

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 914 of Zinc finger protein ZFAT

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 Zinc finger protein ZFAT between cysteines 356 and 359 (67 and 70 respectively in this structure).

Details

Redox score ?
89
PDB code
2rv7
Structure name
solution structures of the dna-binding domains (zf3-zf4-zf5) of immune-related zinc-finger protein zfat
Structure deposition date
2015-01-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
7
% buried
0
Peptide accession
Q9P243
Residue number A
356
Residue number B
359
Peptide name
Zinc finger protein ZFAT

Ligandability

Cysteine 356 of Zinc finger protein ZFAT

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 359 of Zinc finger protein ZFAT

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 Zinc finger protein ZFAT between cysteines 301 and 304 (40 and 43 respectively in this structure).

Details

Redox score ?
88
PDB code
2rv6
Structure name
solution structures of the dna-binding domains (zf2-zf3-zf4) of immune-related zinc-finger protein zfat
Structure deposition date
2015-01-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
7
% buried
0
Peptide accession
Q9P243
Residue number A
301
Residue number B
304
Peptide name
Zinc finger protein ZFAT

Ligandability

Cysteine 301 of Zinc finger protein ZFAT

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 304 of Zinc finger protein ZFAT

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 Zinc finger protein ZFAT between cysteines 772 and 775 (12 and 15 respectively in this structure).

Details

Redox score ?
88
PDB code
2ruy
Structure name
solution structures of the dna-binding domain (zf10) of immune-related zinc-finger protein zfat
Structure deposition date
2015-01-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
7
% buried
0
Peptide accession
Q9P243
Residue number A
772
Residue number B
775
Peptide name
Zinc finger protein ZFAT

Ligandability

Cysteine 772 of Zinc finger protein ZFAT

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 775 of Zinc finger protein ZFAT

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 Zinc finger protein ZFAT between cysteines 832 and 835 (12 and 15 respectively in this structure).

Details

Redox score ?
88
PDB code
2rv0
Structure name
solution structures of the dna-binding domain (zf12) of immune-related zinc-finger protein zfat
Structure deposition date
2015-01-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
7
% buried
0
Peptide accession
Q9P243
Residue number A
832
Residue number B
835
Peptide name
Zinc finger protein ZFAT

Ligandability

Cysteine 832 of Zinc finger protein ZFAT

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 835 of Zinc finger protein ZFAT

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 Zinc finger protein ZFAT between cysteines 406 and 409 (12 and 15 respectively in this structure).

Details

Redox score ?
88
PDB code
2rux
Structure name
solution structures of the dna-binding domain (zf6) of immune-related zinc-finger protein zfat
Structure deposition date
2015-01-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
7
% buried
0
Peptide accession
Q9P243
Residue number A
406
Residue number B
409
Peptide name
Zinc finger protein ZFAT

Ligandability

Cysteine 406 of Zinc finger protein ZFAT

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 409 of Zinc finger protein ZFAT

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 Zinc finger protein ZFAT between cysteines 273 and 276 (12 and 15 respectively in this structure).

Details

Redox score ?
88
PDB code
2rv6
Structure name
solution structures of the dna-binding domains (zf2-zf3-zf4) of immune-related zinc-finger protein zfat
Structure deposition date
2015-01-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
7
% buried
0
Peptide accession
Q9P243
Residue number A
273
Residue number B
276
Peptide name
Zinc finger protein ZFAT

Ligandability

Cysteine 273 of Zinc finger protein ZFAT

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 276 of Zinc finger protein ZFAT

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 Zinc finger protein ZFAT between cysteines 800 and 805 (12 and 17 respectively in this structure).

Details

Redox score ?
88
PDB code
2eln
Structure name
solution structure of the 11th c2h2 zinc finger of human zinc finger protein 406
Structure deposition date
2007-03-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
7
% buried
0
Peptide accession
Q9P243
Residue number A
800
Residue number B
805
Peptide name
Zinc finger protein ZFAT

Ligandability

Cysteine 800 of Zinc finger protein ZFAT

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 805 of Zinc finger protein ZFAT

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 Zinc finger protein ZFAT between cysteines 882 and 885 (12 and 15 respectively in this structure).

Details

Redox score ?
86
PDB code
2elp
Structure name
solution structure of the 13th c2h2 zinc finger of human zinc finger protein 406
Structure deposition date
2007-03-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
35
Minimum pKa ?
7
% buried
0
Peptide accession
Q9P243
Residue number A
882
Residue number B
885
Peptide name
Zinc finger protein ZFAT

Ligandability

Cysteine 882 of Zinc finger protein ZFAT

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 885 of Zinc finger protein ZFAT

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 Zinc finger protein ZFAT between cysteines 328 and 335 (12 and 19 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
2ruv
Structure name
solution structures of the dna-binding domain (zf4) of immune-related zinc-finger protein zfat
Structure deposition date
2015-01-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
45
Minimum pKa ?
7
% buried
0
Peptide accession
Q9P243
Residue number A
328
Residue number B
335
Peptide name
Zinc finger protein ZFAT

Ligandability

Cysteine 328 of Zinc finger protein ZFAT

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 335 of Zinc finger protein ZFAT

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 Zinc finger protein ZFAT between cysteines 276 and 304 (15 and 43 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
2rv6
Structure name
solution structures of the dna-binding domains (zf2-zf3-zf4) of immune-related zinc-finger protein zfat
Structure deposition date
2015-01-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
24
Minimum pKa ?
7
% buried
0
Peptide accession
Q9P243
Residue number A
276
Residue number B
304
Peptide name
Zinc finger protein ZFAT

Ligandability

Cysteine 276 of Zinc finger protein ZFAT

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 304 of Zinc finger protein ZFAT

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 Zinc finger protein ZFAT between cysteines 301 and 335 (12 and 46 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
2rsi
Structure name
solution structures of the dna-binding domains of immune-related zinc- finger protein zfat
Structure deposition date
2012-03-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
50
Minimum pKa ?
7
% buried
0
Peptide accession
Q9P243
Residue number A
301
Residue number B
335
Peptide name
Zinc finger protein ZFAT

Ligandability

Cysteine 301 of Zinc finger protein ZFAT

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 335 of Zinc finger protein ZFAT

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 Zinc finger protein ZFAT between cysteines 331 and 335 (70 and 74 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
2rv6
Structure name
solution structures of the dna-binding domains (zf2-zf3-zf4) of immune-related zinc-finger protein zfat
Structure deposition date
2015-01-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
32
Minimum pKa ?
9
% buried
0
Peptide accession
Q9P243
Residue number A
331
Residue number B
335
Peptide name
Zinc finger protein ZFAT

Ligandability

Cysteine 331 of Zinc finger protein ZFAT

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 335 of Zinc finger protein ZFAT

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 Zinc finger protein ZFAT between cysteines 304 and 335 (43 and 74 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
2rv6
Structure name
solution structures of the dna-binding domains (zf2-zf3-zf4) of immune-related zinc-finger protein zfat
Structure deposition date
2015-01-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
32
Minimum pKa ?
9
% buried
0
Peptide accession
Q9P243
Residue number A
304
Residue number B
335
Peptide name
Zinc finger protein ZFAT

Ligandability

Cysteine 304 of Zinc finger protein ZFAT

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 335 of Zinc finger protein ZFAT

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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