ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase ZFP91

Intramolecular
Cysteine 432 and cysteine 435
Cysteine 402 and cysteine 405
Cysteine 374 and cysteine 377
Cysteine 402 and cysteine 409
Cysteine 405 and cysteine 432
Cysteine 405 and cysteine 409
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase ZFP91 between cysteines 432 and 435 (74 and 77 respectively in this structure).

Details

Redox score ?
84
PDB code
2m9a
Structure name
solution nmr structure of e3 ubiquitin-protein ligase zfp91 from homo sapiens, northeast structural genomics consortium (nesg) target hr7784a
Structure deposition date
2013-06-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
6
% buried
0
Peptide accession
Q96JP5
Residue number A
432
Residue number B
435
Peptide name
E3 ubiquitin-protein ligase ZFP91

Ligandability

Cysteine 432 of E3 ubiquitin-protein ligase ZFP91

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 435 of E3 ubiquitin-protein ligase ZFP91

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 E3 ubiquitin-protein ligase ZFP91 between cysteines 402 and 405 (44 and 47 respectively in this structure).

Details

Redox score ?
84
PDB code
2m9a
Structure name
solution nmr structure of e3 ubiquitin-protein ligase zfp91 from homo sapiens, northeast structural genomics consortium (nesg) target hr7784a
Structure deposition date
2013-06-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
8
% buried
4
Peptide accession
Q96JP5
Residue number A
402
Residue number B
405
Peptide name
E3 ubiquitin-protein ligase ZFP91

Ligandability

Cysteine 402 of E3 ubiquitin-protein ligase ZFP91

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 E3 ubiquitin-protein ligase ZFP91

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 E3 ubiquitin-protein ligase ZFP91 between cysteines 374 and 377 (16 and 19 respectively in this structure).

Details

Redox score ?
82
PDB code
2m9a
Structure name
solution nmr structure of e3 ubiquitin-protein ligase zfp91 from homo sapiens, northeast structural genomics consortium (nesg) target hr7784a
Structure deposition date
2013-06-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
9
% buried
0
Peptide accession
Q96JP5
Residue number A
374
Residue number B
377
Peptide name
E3 ubiquitin-protein ligase ZFP91

Ligandability

Cysteine 374 of E3 ubiquitin-protein ligase ZFP91

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 E3 ubiquitin-protein ligase ZFP91

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 E3 ubiquitin-protein ligase ZFP91 between cysteines 402 and 409 (44 and 51 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
2m9a
Structure name
solution nmr structure of e3 ubiquitin-protein ligase zfp91 from homo sapiens, northeast structural genomics consortium (nesg) target hr7784a
Structure deposition date
2013-06-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
8
% buried
2
Peptide accession
Q96JP5
Residue number A
402
Residue number B
409
Peptide name
E3 ubiquitin-protein ligase ZFP91

Ligandability

Cysteine 402 of E3 ubiquitin-protein ligase ZFP91

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 409 of E3 ubiquitin-protein ligase ZFP91

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 E3 ubiquitin-protein ligase ZFP91 between cysteines 405 and 432 (47 and 74 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
2m9a
Structure name
solution nmr structure of e3 ubiquitin-protein ligase zfp91 from homo sapiens, northeast structural genomics consortium (nesg) target hr7784a
Structure deposition date
2013-06-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
3
Peptide accession
Q96JP5
Residue number A
405
Residue number B
432
Peptide name
E3 ubiquitin-protein ligase ZFP91

Ligandability

Cysteine 405 of E3 ubiquitin-protein ligase ZFP91

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 432 of E3 ubiquitin-protein ligase ZFP91

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 E3 ubiquitin-protein ligase ZFP91 between cysteines 405 and 409 (47 and 51 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2m9a
Structure name
solution nmr structure of e3 ubiquitin-protein ligase zfp91 from homo sapiens, northeast structural genomics consortium (nesg) target hr7784a
Structure deposition date
2013-06-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
39
Minimum pKa ?
8
% buried
4
Peptide accession
Q96JP5
Residue number A
405
Residue number B
409
Peptide name
E3 ubiquitin-protein ligase ZFP91

Ligandability

Cysteine 405 of E3 ubiquitin-protein ligase ZFP91

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 409 of E3 ubiquitin-protein ligase ZFP91

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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