ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Zinc finger protein 483

Intramolecular
Cysteine 392 and cysteine 416
Cysteine 392 and cysteine 395
Cysteine 392 and cysteine 413
Cysteine 395 and cysteine 413
Cysteine 413 and cysteine 416
Cysteine 395 and cysteine 416
Cysteine 392 and cysteine 421
Cysteine 416 and cysteine 421
Cysteine 413 and cysteine 421
Cysteine 395 and cysteine 421
A redox-regulated disulphide may form within Zinc finger protein 483 between cysteines 392 and 416 (21 and 45 respectively in this structure).

Details

Redox score ?
91
PDB code
2ctu
Structure name
solution structure of zinc finger domain from human zn finger protein 483
Structure deposition date
2005-05-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
5
% buried
0
Peptide accession
Q8TF39
Residue number A
392
Residue number B
416
Peptide name
Zinc finger protein 483

Ligandability

Cysteine 392 of Zinc finger protein 483

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 416 of Zinc finger protein 483

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 483 between cysteines 392 and 395 (21 and 24 respectively in this structure).

Details

Redox score ?
90
PDB code
2ctu
Structure name
solution structure of zinc finger domain from human zn finger protein 483
Structure deposition date
2005-05-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
5
% buried
0
Peptide accession
Q8TF39
Residue number A
392
Residue number B
395
Peptide name
Zinc finger protein 483

Ligandability

Cysteine 392 of Zinc finger protein 483

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 395 of Zinc finger protein 483

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 483 between cysteines 392 and 413 (21 and 42 respectively in this structure).

Details

Redox score ?
90
PDB code
2ctu
Structure name
solution structure of zinc finger domain from human zn finger protein 483
Structure deposition date
2005-05-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
5
% buried
0
Peptide accession
Q8TF39
Residue number A
392
Residue number B
413
Peptide name
Zinc finger protein 483

Ligandability

Cysteine 392 of Zinc finger protein 483

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 413 of Zinc finger protein 483

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 483 between cysteines 395 and 413 (24 and 42 respectively in this structure).

Details

Redox score ?
85
PDB code
2ctu
Structure name
solution structure of zinc finger domain from human zn finger protein 483
Structure deposition date
2005-05-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
43
Minimum pKa ?
7
% buried
0
Peptide accession
Q8TF39
Residue number A
395
Residue number B
413
Peptide name
Zinc finger protein 483

Ligandability

Cysteine 395 of Zinc finger protein 483

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 413 of Zinc finger protein 483

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 483 between cysteines 413 and 416 (42 and 45 respectively in this structure).

Details

Redox score ?
84
PDB code
2ctu
Structure name
solution structure of zinc finger domain from human zn finger protein 483
Structure deposition date
2005-05-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
7
% buried
0
Peptide accession
Q8TF39
Residue number A
413
Residue number B
416
Peptide name
Zinc finger protein 483

Ligandability

Cysteine 413 of Zinc finger protein 483

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 416 of Zinc finger protein 483

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 483 between cysteines 395 and 416 (24 and 45 respectively in this structure).

Details

Redox score ?
78
PDB code
2ctu
Structure name
solution structure of zinc finger domain from human zn finger protein 483
Structure deposition date
2005-05-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
9
% buried
0
Peptide accession
Q8TF39
Residue number A
395
Residue number B
416
Peptide name
Zinc finger protein 483

Ligandability

Cysteine 395 of Zinc finger protein 483

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 416 of Zinc finger protein 483

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 483 between cysteines 392 and 421 (21 and 50 respectively in this structure).

Details

Redox score ?
67
PDB code
2ctu
Structure name
solution structure of zinc finger domain from human zn finger protein 483
Structure deposition date
2005-05-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
30
Minimum pKa ?
5
% buried
0
Peptide accession
Q8TF39
Residue number A
392
Residue number B
421
Peptide name
Zinc finger protein 483

Ligandability

Cysteine 392 of Zinc finger protein 483

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 483

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 483 between cysteines 416 and 421 (45 and 50 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
2ctu
Structure name
solution structure of zinc finger domain from human zn finger protein 483
Structure deposition date
2005-05-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
30
Minimum pKa ?
9
% buried
0
Peptide accession
Q8TF39
Residue number A
416
Residue number B
421
Peptide name
Zinc finger protein 483

Ligandability

Cysteine 416 of Zinc finger protein 483

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 483

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 483 between cysteines 413 and 421 (42 and 50 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
2ctu
Structure name
solution structure of zinc finger domain from human zn finger protein 483
Structure deposition date
2005-05-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
35
Minimum pKa ?
7
% buried
0
Peptide accession
Q8TF39
Residue number A
413
Residue number B
421
Peptide name
Zinc finger protein 483

Ligandability

Cysteine 413 of Zinc finger protein 483

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 483

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 483 between cysteines 395 and 421 (24 and 50 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
2ctu
Structure name
solution structure of zinc finger domain from human zn finger protein 483
Structure deposition date
2005-05-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
26
Minimum pKa ?
9
% buried
0
Peptide accession
Q8TF39
Residue number A
395
Residue number B
421
Peptide name
Zinc finger protein 483

Ligandability

Cysteine 395 of Zinc finger protein 483

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 483

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.

If this tool was useful for finding a disulphide, please cite: