ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Zinc finger protein 224

Intramolecular
Cysteine 430 and cysteine 433
Cysteine 654 and cysteine 657
Cysteine 402 and cysteine 573
Cysteine 290 and cysteine 293
Cysteine 346 and cysteine 349
Cysteine 262 and cysteine 265
Cysteine 206 and cysteine 209
Cysteine 318 and cysteine 321
Cysteine 458 and cysteine 461
Cysteine 374 and cysteine 377
More...
Cysteine 682 and cysteine 685
Cysteine 178 and cysteine 181
Cysteine 234 and cysteine 237
Cysteine 402 and cysteine 405
Cysteine 402 and cysteine 415
Cysteine 405 and cysteine 415
Cysteine 682 and cysteine 688
Cysteine 685 and cysteine 688
A redox-regulated disulphide may form within Zinc finger protein 224 between cysteines 430 and 433 (15 and 18 respectively in this structure).

Details

Redox score ?
88
PDB code
2em8
Structure name
solution structure of the c2h2 type zinc finger (region 423-455) of human zinc finger protein 224
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
7
% buried
0
Peptide accession
Q9NZL3
Residue number A
430
Residue number B
433
Peptide name
Zinc finger protein 224

Ligandability

Cysteine 430 of Zinc finger protein 224

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 433 of Zinc finger protein 224

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 224 between cysteines 654 and 657 (15 and 18 respectively in this structure).

Details

Redox score ?
88
PDB code
2elz
Structure name
solution structure of the 17th zf-c2h2 domain from human zinc finger protein 224
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
7
% buried
0
Peptide accession
Q9NZL3
Residue number A
654
Residue number B
657
Peptide name
Zinc finger protein 224

Ligandability

Cysteine 654 of Zinc finger protein 224

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 657 of Zinc finger protein 224

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 224 between cysteines 402 and 573 (15 and 18 respectively in this structure).

Details

Redox score ?
88
PDB code
2en1
Structure name
solution structure of the c2h2 type zinc finger (region 563-595) of human zinc finger protein 224
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
5
% buried
0
Peptide accession
Q9NZL3
Residue number A
402
Residue number B
573
Peptide name
Zinc finger protein 224

Ligandability

Cysteine 402 of Zinc finger protein 224

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 224

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 224 between cysteines 290 and 293 (15 and 18 respectively in this structure).

Details

Redox score ?
87
PDB code
2eoq
Structure name
solution structure of the c2h2 type zinc finger (region 283-315) of human zinc finger protein 224
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
6
% buried
0
Peptide accession
Q9NZL3
Residue number A
290
Residue number B
293
Peptide name
Zinc finger protein 224

Ligandability

Cysteine 290 of Zinc finger protein 224

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 293 of Zinc finger protein 224

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 224 between cysteines 346 and 349 (15 and 18 respectively in this structure).

Details

Redox score ?
87
PDB code
2em7
Structure name
solution structure of the c2h2 type zinc finger (region 339-371) of human zinc finger protein 224
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
6
% buried
0
Peptide accession
Q9NZL3
Residue number A
346
Residue number B
349
Peptide name
Zinc finger protein 224

Ligandability

Cysteine 346 of Zinc finger protein 224

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 349 of Zinc finger protein 224

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 224 between cysteines 262 and 265 (15 and 18 respectively in this structure).

Details

Redox score ?
87
PDB code
2eor
Structure name
solution structure of the c2h2 type zinc finger (region 255-287) of human zinc finger protein 224
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
7
% buried
0
Peptide accession
Q9NZL3
Residue number A
262
Residue number B
265
Peptide name
Zinc finger protein 224

Ligandability

Cysteine 262 of Zinc finger protein 224

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 265 of Zinc finger protein 224

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 224 between cysteines 206 and 209 (15 and 18 respectively in this structure).

Details

Redox score ?
87
PDB code
2em6
Structure name
solution structure of the c2h2 type zinc finger (region 199-231) of human zinc finger protein 224
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
35
Minimum pKa ?
7
% buried
0
Peptide accession
Q9NZL3
Residue number A
206
Residue number B
209
Peptide name
Zinc finger protein 224

Ligandability

Cysteine 206 of Zinc finger protein 224

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 209 of Zinc finger protein 224

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 224 between cysteines 318 and 321 (15 and 18 respectively in this structure).

Details

Redox score ?
86
PDB code
2ena
Structure name
solution structure of the c2h2 type zinc finger (region 311-343) of human zinc finger protein 224
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
6
% buried
0
Peptide accession
Q9NZL3
Residue number A
318
Residue number B
321
Peptide name
Zinc finger protein 224

Ligandability

Cysteine 318 of Zinc finger protein 224

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 Zinc finger protein 224

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 224 between cysteines 458 and 461.

Details

Redox score ?
86
PDB code
2eq4
Structure name
solution structure of the 11th c2h2 type zinc finger domain of zinc finger protein 224
Structure deposition date
2007-03-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
8
% buried
0
Peptide accession
Q9NZL3
Residue number A
458
Residue number B
461
Peptide name
Zinc finger protein 224

Ligandability

Cysteine 458 of Zinc finger protein 224

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 461 of Zinc finger protein 224

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 224 between cysteines 374 and 377 (15 and 18 respectively in this structure).

Details

Redox score ?
85
PDB code
2em9
Structure name
solution structure of the c2h2 type zinc finger (region 367-399) of human zinc finger protein 224
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
35
Minimum pKa ?
8
% buried
0
Peptide accession
Q9NZL3
Residue number A
374
Residue number B
377
Peptide name
Zinc finger protein 224

Ligandability

Cysteine 374 of Zinc finger protein 224

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 377 of Zinc finger protein 224

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 224 between cysteines 682 and 685 (15 and 18 respectively in this structure).

Details

Redox score ?
85
PDB code
2em0
Structure name
solution structure of the 18th zf-c2h2 domain from human zinc finger protein 224
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
8
% buried
0
Peptide accession
Q9NZL3
Residue number A
682
Residue number B
685
Peptide name
Zinc finger protein 224

Ligandability

Cysteine 682 of Zinc finger protein 224

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 685 of Zinc finger protein 224

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 224 between cysteines 178 and 181 (15 and 18 respectively in this structure).

Details

Redox score ?
84
PDB code
2en8
Structure name
solution structure of the c2h2 type zinc finger (region 171-203) of human zinc finger protein 224
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
8
% buried
0
Peptide accession
Q9NZL3
Residue number A
178
Residue number B
181
Peptide name
Zinc finger protein 224

Ligandability

Cysteine 178 of Zinc finger protein 224

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 181 of Zinc finger protein 224

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 224 between cysteines 234 and 237 (15 and 18 respectively in this structure).

Details

Redox score ?
84
PDB code
2ely
Structure name
solution structure of the third zf-c2h2 domain from human zinc finger protein 224
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
8
% buried
0
Peptide accession
Q9NZL3
Residue number A
234
Residue number B
237
Peptide name
Zinc finger protein 224

Ligandability

Cysteine 234 of Zinc finger protein 224

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 237 of Zinc finger protein 224

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 224 between cysteines 402 and 405 (15 and 18 respectively in this structure).

Details

Redox score ?
83
PDB code
2enc
Structure name
solution structure of the c2h2 type zinc finger (region 395-427) of human zinc finger protein 224
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
8
% buried
0
Peptide accession
Q9NZL3
Residue number A
402
Residue number B
405
Peptide name
Zinc finger protein 224

Ligandability

Cysteine 402 of Zinc finger protein 224

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 405 of Zinc finger protein 224

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 224 between cysteines 402 and 415 (15 and 28 respectively in this structure).

Details

Redox score ?
72
PDB code
2enc
Structure name
solution structure of the c2h2 type zinc finger (region 395-427) of human zinc finger protein 224
Structure deposition date
2007-03-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
0
Peptide accession
Q9NZL3
Residue number A
402
Residue number B
415
Peptide name
Zinc finger protein 224

Ligandability

Cysteine 402 of Zinc finger protein 224

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 415 of Zinc finger protein 224

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 224 between cysteines 405 and 415 (18 and 28 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
2enc
Structure name
solution structure of the c2h2 type zinc finger (region 395-427) of human zinc finger protein 224
Structure deposition date
2007-03-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
37
Minimum pKa ?
8
% buried
0
Peptide accession
Q9NZL3
Residue number A
405
Residue number B
415
Peptide name
Zinc finger protein 224

Ligandability

Cysteine 405 of Zinc finger protein 224

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 415 of Zinc finger protein 224

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 224 between cysteines 682 and 688 (15 and 21 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
2em0
Structure name
solution structure of the 18th zf-c2h2 domain from human zinc finger protein 224
Structure deposition date
2007-03-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
0
Peptide accession
Q9NZL3
Residue number A
682
Residue number B
688
Peptide name
Zinc finger protein 224

Ligandability

Cysteine 682 of Zinc finger protein 224

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 688 of Zinc finger protein 224

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 224 between cysteines 685 and 688 (18 and 21 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
2em0
Structure name
solution structure of the 18th zf-c2h2 domain from human zinc finger protein 224
Structure deposition date
2007-03-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
39
Minimum pKa ?
9
% buried
0
Peptide accession
Q9NZL3
Residue number A
685
Residue number B
688
Peptide name
Zinc finger protein 224

Ligandability

Cysteine 685 of Zinc finger protein 224

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 688 of Zinc finger protein 224

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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