ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Zinc finger protein 484

Intramolecular
Cysteine 610 and cysteine 613
Cysteine 498 and cysteine 501
Cysteine 414 and cysteine 417
Cysteine 526 and cysteine 529
Cysteine 470 and cysteine 473
Cysteine 442 and cysteine 445
Cysteine 638 and cysteine 641
Cysteine 554 and cysteine 557
Cysteine 386 and cysteine 389
Cysteine 526 and cysteine 545
Cysteine 529 and cysteine 545
A redox-regulated disulphide may form within Zinc finger protein 484 between cysteines 610 and 613 (15 and 18 respectively in this structure).

Details

Redox score ?
90
PDB code
2ep2
Structure name
solution structure of the c2h2 type zinc finger (region 603-635) of human zinc finger protein 484
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
6
% buried
0
Peptide accession
Q5JVG2
Residue number A
610
Residue number B
613
Peptide name
Zinc finger protein 484

Ligandability

Cysteine 610 of Zinc finger protein 484

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 613 of Zinc finger protein 484

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 484 between cysteines 498 and 501 (15 and 18 respectively in this structure).

Details

Redox score ?
88
PDB code
2emh
Structure name
solution structure of the c2h2 type zinc finger (region 491-523) of human zinc finger protein 484
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
7
% buried
0
Peptide accession
Q5JVG2
Residue number A
498
Residue number B
501
Peptide name
Zinc finger protein 484

Ligandability

Cysteine 498 of Zinc finger protein 484

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 501 of Zinc finger protein 484

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 484 between cysteines 414 and 417.

Details

Redox score ?
87
PDB code
2eqw
Structure name
solution structure of the 6th c2h2 type zinc finger domain of zinc finger protein 484
Structure deposition date
2007-03-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
34
Minimum pKa ?
7
% buried
0
Peptide accession
Q5JVG2
Residue number A
414
Residue number B
417
Peptide name
Zinc finger protein 484

Ligandability

Cysteine 414 of Zinc finger protein 484

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 417 of Zinc finger protein 484

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 484 between cysteines 526 and 529 (15 and 18 respectively in this structure).

Details

Redox score ?
86
PDB code
2eov
Structure name
solution structure of the c2h2 type zinc finger (region 519-551) of human zinc finger protein 484
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
7
% buried
0
Peptide accession
Q5JVG2
Residue number A
526
Residue number B
529
Peptide name
Zinc finger protein 484

Ligandability

Cysteine 526 of Zinc finger protein 484

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 529 of Zinc finger protein 484

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 484 between cysteines 470 and 473 (15 and 18 respectively in this structure).

Details

Redox score ?
85
PDB code
2emg
Structure name
solution structure of the c2h2 type zinc finger (region 463-495) of human zinc finger protein 484
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
8
% buried
0
Peptide accession
Q5JVG2
Residue number A
470
Residue number B
473
Peptide name
Zinc finger protein 484

Ligandability

Cysteine 470 of Zinc finger protein 484

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 473 of Zinc finger protein 484

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 484 between cysteines 442 and 445 (15 and 18 respectively in this structure).

Details

Redox score ?
85
PDB code
2ep1
Structure name
solution structure of the c2h2 type zinc finger (region 435-467) of human zinc finger protein 484
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
8
% buried
0
Peptide accession
Q5JVG2
Residue number A
442
Residue number B
445
Peptide name
Zinc finger protein 484

Ligandability

Cysteine 442 of Zinc finger protein 484

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 445 of Zinc finger protein 484

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 484 between cysteines 638 and 641 (15 and 18 respectively in this structure).

Details

Redox score ?
85
PDB code
2ep3
Structure name
solution structure of the c2h2 type zinc finger (region 631-663) of human zinc finger protein 484
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
35
Minimum pKa ?
8
% buried
0
Peptide accession
Q5JVG2
Residue number A
638
Residue number B
641
Peptide name
Zinc finger protein 484

Ligandability

Cysteine 638 of Zinc finger protein 484

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 641 of Zinc finger protein 484

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 484 between cysteines 554 and 557 (15 and 18 respectively in this structure).

Details

Redox score ?
85
PDB code
2emi
Structure name
solution structure of the c2h2 type zinc finger (region 547-579) of human zinc finger protein 484
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
8
% buried
0
Peptide accession
Q5JVG2
Residue number A
554
Residue number B
557
Peptide name
Zinc finger protein 484

Ligandability

Cysteine 554 of Zinc finger protein 484

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 557 of Zinc finger protein 484

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 484 between cysteines 386 and 389 (15 and 18 respectively in this structure).

Details

Redox score ?
84
PDB code
2emf
Structure name
solution structure of the c2h2 type zinc finger (region 379-411) of human zinc finger protein 484
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
8
% buried
0
Peptide accession
Q5JVG2
Residue number A
386
Residue number B
389
Peptide name
Zinc finger protein 484

Ligandability

Cysteine 386 of Zinc finger protein 484

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 389 of Zinc finger protein 484

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 484 between cysteines 526 and 545 (15 and 34 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
2eov
Structure name
solution structure of the c2h2 type zinc finger (region 519-551) of human zinc finger protein 484
Structure deposition date
2007-03-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
41
Minimum pKa ?
7
% buried
0
Peptide accession
Q5JVG2
Residue number A
526
Residue number B
545
Peptide name
Zinc finger protein 484

Ligandability

Cysteine 526 of Zinc finger protein 484

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 545 of Zinc finger protein 484

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 484 between cysteines 529 and 545 (18 and 34 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
2eov
Structure name
solution structure of the c2h2 type zinc finger (region 519-551) of human zinc finger protein 484
Structure deposition date
2007-03-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
32
Minimum pKa ?
9
% buried
0
Peptide accession
Q5JVG2
Residue number A
529
Residue number B
545
Peptide name
Zinc finger protein 484

Ligandability

Cysteine 529 of Zinc finger protein 484

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 545 of Zinc finger protein 484

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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