ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Zinc finger protein 473

Intramolecular
Cysteine 816 and cysteine 819
Cysteine 648 and cysteine 651
Cysteine 349 and cysteine 352
Cysteine 564 and cysteine 567
Cysteine 732 and cysteine 735
Cysteine 322 and cysteine 325
Cysteine 377 and cysteine 380
Cysteine 561 and cysteine 573
A redox-regulated disulphide may form within Zinc finger protein 473 between cysteines 816 and 819 (15 and 18 respectively in this structure).

Details

Redox score ?
90
PDB code
2eoz
Structure name
solution structure of the c2h2 type zinc finger (region 809-841) of human zinc finger protein 473
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
6
% buried
0
Peptide accession
Q8WTR7
Residue number A
816
Residue number B
819
Peptide name
Zinc finger protein 473

Ligandability

Cysteine 816 of Zinc finger protein 473

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 819 of Zinc finger protein 473

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 473 between cysteines 648 and 651 (15 and 18 respectively in this structure).

Details

Redox score ?
89
PDB code
2emc
Structure name
solution structure of the c2h2 type zinc finger (region 641-673) of human zinc finger protein 473
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
7
% buried
0
Peptide accession
Q8WTR7
Residue number A
648
Residue number B
651
Peptide name
Zinc finger protein 473

Ligandability

Cysteine 648 of Zinc finger protein 473

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 651 of Zinc finger protein 473

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 473 between cysteines 349 and 352 (15 and 18 respectively in this structure).

Details

Redox score ?
87
PDB code
2emb
Structure name
solution structure of the c2h2 type zinc finger (region 342-372) of human zinc finger protein 473
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
34
Minimum pKa ?
7
% buried
0
Peptide accession
Q8WTR7
Residue number A
349
Residue number B
352
Peptide name
Zinc finger protein 473

Ligandability

Cysteine 349 of Zinc finger protein 473

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 352 of Zinc finger protein 473

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 473 between cysteines 564 and 567 (15 and 18 respectively in this structure).

Details

Redox score ?
86
PDB code
2eoy
Structure name
solution structure of the c2h2 type zinc finger (region 557-589) of human zinc finger protein 473
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
8
% buried
0
Peptide accession
Q8WTR7
Residue number A
564
Residue number B
567
Peptide name
Zinc finger protein 473

Ligandability

Cysteine 564 of Zinc finger protein 473

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 567 of Zinc finger protein 473

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 473 between cysteines 732 and 735 (15 and 18 respectively in this structure).

Details

Redox score ?
86
PDB code
2eme
Structure name
solution structure of the c2h2 type zinc finger (region 725-757) of human zinc finger protein 473
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
7
% buried
0
Peptide accession
Q8WTR7
Residue number A
732
Residue number B
735
Peptide name
Zinc finger protein 473

Ligandability

Cysteine 732 of Zinc finger protein 473

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 735 of Zinc finger protein 473

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 473 between cysteines 322 and 325 (15 and 18 respectively in this structure).

Details

Redox score ?
85
PDB code
2eox
Structure name
solution structure of the c2h2 type zinc finger (region 315-345) of human zinc finger protein 473
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
35
Minimum pKa ?
8
% buried
0
Peptide accession
Q8WTR7
Residue number A
322
Residue number B
325
Peptide name
Zinc finger protein 473

Ligandability

Cysteine 322 of Zinc finger protein 473

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 325 of Zinc finger protein 473

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 473 between cysteines 377 and 380 (15 and 18 respectively in this structure).

Details

Redox score ?
81
PDB code
2eou
Structure name
solution structure of the c2h2 type zinc finger (region 370-400) of human zinc finger protein 473
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
0
Peptide accession
Q8WTR7
Residue number A
377
Residue number B
380
Peptide name
Zinc finger protein 473

Ligandability

Cysteine 377 of Zinc finger protein 473

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 380 of Zinc finger protein 473

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 473 between cysteines 561 and 573 (12 and 24 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
2eoy
Structure name
solution structure of the c2h2 type zinc finger (region 557-589) of human zinc finger protein 473
Structure deposition date
2007-03-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
31
Minimum pKa ?
9
% buried
0
Peptide accession
Q8WTR7
Residue number A
561
Residue number B
573
Peptide name
Zinc finger protein 473

Ligandability

Cysteine 561 of Zinc finger protein 473

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 573 of Zinc finger protein 473

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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