ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Zinc finger protein 28 homolog

Intramolecular
Cysteine 647 and cysteine 650
Cysteine 591 and cysteine 594
Cysteine 787 and cysteine 790
Cysteine 619 and cysteine 622
Cysteine 507 and cysteine 510
Cysteine 731 and cysteine 734
Cysteine 535 and cysteine 538
Cysteine 422 and cysteine 425
Cysteine 563 and cysteine 566
Cysteine 675 and cysteine 678
More...
Cysteine 478 and cysteine 481
Cysteine 759 and cysteine 762
A redox-regulated disulphide may form within Zinc finger protein 28 homolog between cysteines 647 and 650 (15 and 18 respectively in this structure).

Details

Redox score ?
88
PDB code
2em3
Structure name
solution structure of the c2h2 type zinc finger (region 640-672) of human zinc finger protein 28 homolog
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
6
% buried
0
Peptide accession
Q8NHY6
Residue number A
647
Residue number B
650
Peptide name
Zinc finger protein 28 homolog

Ligandability

Cysteine 647 of Zinc finger protein 28 homolog

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 650 of Zinc finger protein 28 homolog

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 28 homolog between cysteines 591 and 594 (15 and 18 respectively in this structure).

Details

Redox score ?
87
PDB code
2em2
Structure name
solution structure of the c2h2 type zinc finger (region 584-616) of human zinc finger protein 28 homolog
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
34
Minimum pKa ?
7
% buried
0
Peptide accession
Q8NHY6
Residue number A
591
Residue number B
594
Peptide name
Zinc finger protein 28 homolog

Ligandability

Cysteine 591 of Zinc finger protein 28 homolog

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 594 of Zinc finger protein 28 homolog

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 28 homolog between cysteines 787 and 790 (15 and 18 respectively in this structure).

Details

Redox score ?
87
PDB code
2eoh
Structure name
solution structure of the c2h2 type zinc finger (region 780-812) of human zinc finger protein 28 homolog
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
6
% buried
0
Peptide accession
Q8NHY6
Residue number A
787
Residue number B
790
Peptide name
Zinc finger protein 28 homolog

Ligandability

Cysteine 787 of Zinc finger protein 28 homolog

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 790 of Zinc finger protein 28 homolog

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 28 homolog between cysteines 619 and 622 (15 and 18 respectively in this structure).

Details

Redox score ?
87
PDB code
2emj
Structure name
solution structure of the c2h2 type zinc finger (region 612-644) of human zinc finger protein 28 homolog
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
34
Minimum pKa ?
7
% buried
0
Peptide accession
Q8NHY6
Residue number A
619
Residue number B
622
Peptide name
Zinc finger protein 28 homolog

Ligandability

Cysteine 619 of Zinc finger protein 28 homolog

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 622 of Zinc finger protein 28 homolog

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 28 homolog between cysteines 507 and 510.

Details

Redox score ?
86
PDB code
2epz
Structure name
solution structure of the 4th c2h2 type zinc finger domain of zinc finger protein 28 homolog
Structure deposition date
2007-03-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
7
% buried
0
Peptide accession
Q8NHY6
Residue number A
507
Residue number B
510
Peptide name
Zinc finger protein 28 homolog

Ligandability

Cysteine 507 of Zinc finger protein 28 homolog

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 510 of Zinc finger protein 28 homolog

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 28 homolog between cysteines 731 and 734 (15 and 18 respectively in this structure).

Details

Redox score ?
86
PDB code
2em4
Structure name
solution structure of the c2h2 type zinc finger (region 724-756) of human zinc finger protein 28 homolog
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
6
% buried
0
Peptide accession
Q8NHY6
Residue number A
731
Residue number B
734
Peptide name
Zinc finger protein 28 homolog

Ligandability

Cysteine 731 of Zinc finger protein 28 homolog

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 734 of Zinc finger protein 28 homolog

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 28 homolog between cysteines 535 and 538 (15 and 18 respectively in this structure).

Details

Redox score ?
86
PDB code
2ep0
Structure name
solution structure of the c2h2 type zinc finger (region 528-560) of human zinc finger protein 28 homolog
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
7
% buried
0
Peptide accession
Q8NHY6
Residue number A
535
Residue number B
538
Peptide name
Zinc finger protein 28 homolog

Ligandability

Cysteine 535 of Zinc finger protein 28 homolog

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 538 of Zinc finger protein 28 homolog

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 28 homolog between cysteines 422 and 425 (15 and 18 respectively in this structure).

Details

Redox score ?
86
PDB code
2en9
Structure name
solution structure of the c2h2 type zinc finger (region 415-447) of human zinc finger protein 28 homolog
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
34
Minimum pKa ?
7
% buried
0
Peptide accession
Q8NHY6
Residue number A
422
Residue number B
425
Peptide name
Zinc finger protein 28 homolog

Ligandability

Cysteine 422 of Zinc finger protein 28 homolog

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 425 of Zinc finger protein 28 homolog

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 28 homolog between cysteines 563 and 566 (15 and 18 respectively in this structure).

Details

Redox score ?
86
PDB code
2enh
Structure name
solution structure of the c2h2 type zinc finger (region 556-588) of human zinc finger protein 28 homolog
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
7
% buried
0
Peptide accession
Q8NHY6
Residue number A
563
Residue number B
566
Peptide name
Zinc finger protein 28 homolog

Ligandability

Cysteine 563 of Zinc finger protein 28 homolog

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 566 of Zinc finger protein 28 homolog

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 28 homolog between cysteines 675 and 678 (15 and 18 respectively in this structure).

Details

Redox score ?
85
PDB code
2emk
Structure name
solution structure of the c2h2 type zinc finger (region 668-700) of human zinc finger protein 28 homolog
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
35
Minimum pKa ?
7
% buried
0
Peptide accession
Q8NHY6
Residue number A
675
Residue number B
678
Peptide name
Zinc finger protein 28 homolog

Ligandability

Cysteine 675 of Zinc finger protein 28 homolog

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 678 of Zinc finger protein 28 homolog

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 28 homolog between cysteines 478 and 481.

Details

Redox score ?
84
PDB code
2epx
Structure name
solution structure of the third c2h2 type zinc finger domain of zinc finger protein 28 homolog
Structure deposition date
2007-03-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
8
% buried
0
Peptide accession
Q8NHY6
Residue number A
478
Residue number B
481
Peptide name
Zinc finger protein 28 homolog

Ligandability

Cysteine 478 of Zinc finger protein 28 homolog

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 481 of Zinc finger protein 28 homolog

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 28 homolog between cysteines 759 and 762 (15 and 18 respectively in this structure).

Details

Redox score ?
83
PDB code
2eml
Structure name
solution structure of the c2h2 type zinc finger (region 752-784) of human zinc finger protein 28 homolog
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
8
% buried
0
Peptide accession
Q8NHY6
Residue number A
759
Residue number B
762
Peptide name
Zinc finger protein 28 homolog

Ligandability

Cysteine 759 of Zinc finger protein 28 homolog

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 762 of Zinc finger protein 28 homolog

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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