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a tool for identifying drug-targetable redox-active disulphides

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Zinc finger protein 268

Intramolecular
Cysteine 278 and cysteine 281
Cysteine 446 and cysteine 449
Cysteine 334 and cysteine 337
Cysteine 642 and cysteine 645
Cysteine 754 and cysteine 757
Cysteine 838 and cysteine 841
Cysteine 670 and cysteine 673
Cysteine 810 and cysteine 813
Cysteine 698 and cysteine 701
Cysteine 418 and cysteine 421
More...
Cysteine 726 and cysteine 729
Cysteine 922 and cysteine 925
Cysteine 558 and cysteine 561
Cysteine 586 and cysteine 589
Cysteine 306 and cysteine 897
Cysteine 306 and cysteine 309
Cysteine 866 and cysteine 869
Cysteine 530 and cysteine 533
Cysteine 362 and cysteine 365
Cysteine 502 and cysteine 505
Cysteine 390 and cysteine 393
Cysteine 278 and cysteine 280
Cysteine 280 and cysteine 281
Cysteine 362 and cysteine 363
Cysteine 363 and cysteine 365
Cysteine 920 and cysteine 922
Cysteine 920 and cysteine 930
A redox-regulated disulphide may form within Zinc finger protein 268 between cysteines 278 and 281 (13 and 16 respectively in this structure).

Details

Redox score ?
92
PDB code
2emx
Structure name
solution structure of the c2h2 type zinc finger (region 273-303) of human zinc finger protein 268
Structure deposition date
2007-03-28
Thiol separation (Å)
3
Half-sphere exposure sum ?
38
Minimum pKa ?
6
% buried
0
Peptide accession
Q14587
Residue number A
278
Residue number B
281
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 278 of Zinc finger protein 268

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 281 of Zinc finger protein 268

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 268 between cysteines 446 and 449 (13 and 16 respectively in this structure).

Details

Redox score ?
90
PDB code
2eok
Structure name
solution structure of the c2h2 type zinc finger (region 441-469) of human zinc finger protein 268
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
6
% buried
0
Peptide accession
Q14587
Residue number A
446
Residue number B
449
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 446 of Zinc finger protein 268

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 449 of Zinc finger protein 268

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 268 between cysteines 334 and 337 (13 and 16 respectively in this structure).

Details

Redox score ?
88
PDB code
2eoi
Structure name
solution structure of the c2h2 type zinc finger (region 329-359) of human zinc finger protein 268
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
6
% buried
0
Peptide accession
Q14587
Residue number A
334
Residue number B
337
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 334 of Zinc finger protein 268

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 337 of Zinc finger protein 268

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 268 between cysteines 642 and 645 (13 and 16 respectively in this structure).

Details

Redox score ?
88
PDB code
2em1
Structure name
solution structure of the c2h2 type zinc finger (region 637-667) of human zinc finger protein 268
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
6
% buried
0
Peptide accession
Q14587
Residue number A
642
Residue number B
645
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 642 of Zinc finger protein 268

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 645 of Zinc finger protein 268

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 268 between cysteines 754 and 757 (13 and 16 respectively in this structure).

Details

Redox score ?
87
PDB code
2el5
Structure name
solution structure of the 18th zf-c2h2 domain from human zinc finger protein 268
Structure deposition date
2007-03-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
34
Minimum pKa ?
7
% buried
0
Peptide accession
Q14587
Residue number A
754
Residue number B
757
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 754 of Zinc finger protein 268

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 757 of Zinc finger protein 268

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 268 between cysteines 838 and 841 (15 and 18 respectively in this structure).

Details

Redox score ?
87
PDB code
2el6
Structure name
solution structure of the 21th zf-c2h2 domain from human zinc finger protein 268
Structure deposition date
2007-03-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
7
% buried
0
Peptide accession
Q14587
Residue number A
838
Residue number B
841
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 838 of Zinc finger protein 268

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 841 of Zinc finger protein 268

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 268 between cysteines 670 and 673 (15 and 18 respectively in this structure).

Details

Redox score ?
87
PDB code
2el4
Structure name
solution structure of the 15th zf-c2h2 domain from human zinc finger protein 268
Structure deposition date
2007-03-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
7
% buried
0
Peptide accession
Q14587
Residue number A
670
Residue number B
673
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 670 of Zinc finger protein 268

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 673 of Zinc finger protein 268

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 268 between cysteines 810 and 813.

Details

Redox score ?
87
PDB code
2epv
Structure name
solution structure of the 20th c2h2 type zinc finger domain of zinc finger protein 268
Structure deposition date
2007-03-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
7
% buried
0
Peptide accession
Q14587
Residue number A
810
Residue number B
813
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 810 of Zinc finger protein 268

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 813 of Zinc finger protein 268

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 268 between cysteines 698 and 701 (13 and 16 respectively in this structure).

Details

Redox score ?
86
PDB code
2eog
Structure name
solution structure of the c2h2 type zinc finger (region 693-723) of human zinc finger protein 268
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
7
% buried
0
Peptide accession
Q14587
Residue number A
698
Residue number B
701
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 698 of Zinc finger protein 268

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 701 of Zinc finger protein 268

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 268 between cysteines 418 and 421 (15 and 18 respectively in this structure).

Details

Redox score ?
86
PDB code
2eof
Structure name
solution structure of the c2h2 type zinc finger (region 411-441) of human zinc finger protein 268
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
7
% buried
0
Peptide accession
Q14587
Residue number A
418
Residue number B
421
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 418 of Zinc finger protein 268

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 421 of Zinc finger protein 268

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 268 between cysteines 726 and 729 (15 and 18 respectively in this structure).

Details

Redox score ?
86
PDB code
2eop
Structure name
solution structure of the c2h2 type zinc finger (region 719-751) of human zinc finger protein 268
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
6
% buried
0
Peptide accession
Q14587
Residue number A
726
Residue number B
729
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 726 of Zinc finger protein 268

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 729 of Zinc finger protein 268

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 268 between cysteines 922 and 925.

Details

Redox score ?
86
PDB code
2epw
Structure name
solution structure of the 24th c2h2 type zinc finger domain of zinc finger protein 268
Structure deposition date
2007-03-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
8
% buried
0
Peptide accession
Q14587
Residue number A
922
Residue number B
925
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 922 of Zinc finger protein 268

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 925 of Zinc finger protein 268

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 268 between cysteines 558 and 561 (15 and 18 respectively in this structure).

Details

Redox score ?
85
PDB code
2emy
Structure name
solution structure of the c2h2 type zinc finger (region 551-583) of human zinc finger protein 268
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
7
% buried
0
Peptide accession
Q14587
Residue number A
558
Residue number B
561
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 558 of Zinc finger protein 268

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 561 of Zinc finger protein 268

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 268 between cysteines 586 and 589 (13 and 16 respectively in this structure).

Details

Redox score ?
85
PDB code
2eol
Structure name
solution structure of the c2h2 type zinc finger (region 581-609) of human zinc finger protein 268
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
8
% buried
0
Peptide accession
Q14587
Residue number A
586
Residue number B
589
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 586 of Zinc finger protein 268

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 589 of Zinc finger protein 268

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 268 between cysteines 306 and 897 (15 and 18 respectively in this structure).

Details

Redox score ?
85
PDB code
2en6
Structure name
solution structure of the c2h2 type zinc finger (region 887-919) of human zinc finger protein 268
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
8
% buried
0
Peptide accession
Q14587
Residue number A
306
Residue number B
897
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 306 of Zinc finger protein 268

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 897 of Zinc finger protein 268

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 268 between cysteines 306 and 309 (13 and 16 respectively in this structure).

Details

Redox score ?
85
PDB code
2emw
Structure name
solution structure of the c2h2 type zinc finger (region 301-331) of human zinc finger protein 268
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
8
% buried
0
Peptide accession
Q14587
Residue number A
306
Residue number B
309
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 306 of Zinc finger protein 268

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 309 of Zinc finger protein 268

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 268 between cysteines 866 and 869 (15 and 18 respectively in this structure).

Details

Redox score ?
85
PDB code
2emv
Structure name
solution structure of the c2h2 type zinc finger (region 859-889) of human zinc finger protein 268
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
7
% buried
0
Peptide accession
Q14587
Residue number A
866
Residue number B
869
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 866 of Zinc finger protein 268

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 869 of Zinc finger protein 268

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 268 between cysteines 530 and 533.

Details

Redox score ?
84
PDB code
2epy
Structure name
solution structure of the 10th c2h2 type zinc finger domain of zinc finger protein 268
Structure deposition date
2007-03-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
8
% buried
0
Peptide accession
Q14587
Residue number A
530
Residue number B
533
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 530 of Zinc finger protein 268

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 533 of Zinc finger protein 268

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 268 between cysteines 362 and 365 (15 and 18 respectively in this structure).

Details

Redox score ?
84
PDB code
2eoj
Structure name
solution structure of the c2h2 type zinc finger (region 355-385) of human zinc finger protein 268
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
8
% buried
0
Peptide accession
Q14587
Residue number A
362
Residue number B
365
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 362 of Zinc finger protein 268

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 365 of Zinc finger protein 268

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 268 between cysteines 502 and 505 (15 and 18 respectively in this structure).

Details

Redox score ?
83
PDB code
2en7
Structure name
solution structure of the c2h2 type zinc finger (region 495-525) of human zinc finger protein 268
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
8
% buried
0
Peptide accession
Q14587
Residue number A
502
Residue number B
505
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 502 of Zinc finger protein 268

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 505 of Zinc finger protein 268

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 268 between cysteines 390 and 393 (13 and 16 respectively in this structure).

Details

Redox score ?
83
PDB code
2en0
Structure name
solution structure of the c2h2 type zinc finger (region 385-413) of human zinc finger protein 268
Structure deposition date
2007-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
8
% buried
0
Peptide accession
Q14587
Residue number A
390
Residue number B
393
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 390 of Zinc finger protein 268

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 393 of Zinc finger protein 268

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 268 between cysteines 278 and 280 (13 and 15 respectively in this structure).

Details

Redox score ?
82
PDB code
2emx
Structure name
solution structure of the c2h2 type zinc finger (region 273-303) of human zinc finger protein 268
Structure deposition date
2007-03-28
Thiol separation (Å)
5
Half-sphere exposure sum ?
39
Minimum pKa ?
6
% buried
0
Peptide accession
Q14587
Residue number A
278
Residue number B
280
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 278 of Zinc finger protein 268

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 280 of Zinc finger protein 268

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 268 between cysteines 280 and 281 (15 and 16 respectively in this structure).

Details

Redox score ?
64
PDB code
2emx
Structure name
solution structure of the c2h2 type zinc finger (region 273-303) of human zinc finger protein 268
Structure deposition date
2007-03-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
29
Minimum pKa ?
9
% buried
0
Peptide accession
Q14587
Residue number A
280
Residue number B
281
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 280 of Zinc finger protein 268

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 281 of Zinc finger protein 268

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 268 between cysteines 362 and 363 (15 and 16 respectively in this structure).

Details

Redox score ?
61
PDB code
2eoj
Structure name
solution structure of the c2h2 type zinc finger (region 355-385) of human zinc finger protein 268
Structure deposition date
2007-03-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
42
Minimum pKa ?
8
% buried
0
Peptide accession
Q14587
Residue number A
362
Residue number B
363
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 362 of Zinc finger protein 268

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 363 of Zinc finger protein 268

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 268 between cysteines 363 and 365 (16 and 18 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2eoj
Structure name
solution structure of the c2h2 type zinc finger (region 355-385) of human zinc finger protein 268
Structure deposition date
2007-03-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
30
Minimum pKa ?
9
% buried
0
Peptide accession
Q14587
Residue number A
363
Residue number B
365
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 363 of Zinc finger protein 268

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 365 of Zinc finger protein 268

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 268 between cysteines 920 and 922. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
2epw
Structure name
solution structure of the 24th c2h2 type zinc finger domain of zinc finger protein 268
Structure deposition date
2007-03-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
39
Minimum pKa ?
8
% buried
0
Peptide accession
Q14587
Residue number A
920
Residue number B
922
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 920 of Zinc finger protein 268

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 922 of Zinc finger protein 268

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 268 between cysteines 920 and 930. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2epw
Structure name
solution structure of the 24th c2h2 type zinc finger domain of zinc finger protein 268
Structure deposition date
2007-03-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
36
Minimum pKa ?
9
% buried
0
Peptide accession
Q14587
Residue number A
920
Residue number B
930
Peptide name
Zinc finger protein 268

Ligandability

Cysteine 920 of Zinc finger protein 268

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 930 of Zinc finger protein 268

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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