ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Nuclear protein localization protein 4 homolog

Intramolecular
Cysteine 586 and cysteine 600
Cysteine 130 and cysteine 138
Cysteine 586 and cysteine 589
Cysteine 138 and cysteine 141
Cysteine 130 and cysteine 141
Cysteine 586 and cysteine 603
Cysteine 600 and cysteine 603
Cysteine 341 and cysteine 399
Cysteine 589 and cysteine 600
Cysteine 589 and cysteine 603
Cysteine 341 and cysteine 391
A redox-regulated disulphide may form within Nuclear protein localization protein 4 homolog between cysteines 586 and 600 (9 and 23 respectively in this structure).

Details

Redox score ?
92
PDB code
1nj3
Structure name
structure and ubiquitin interactions of the conserved nzf domain of npl4
Structure deposition date
2002-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
0
Peptide accession
Q9ES54
Residue number A
586
Residue number B
600
Peptide name
Nuclear protein localization protein 4 homolog

Ligandability

Cysteine 586 of Nuclear protein localization protein 4 homolog

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 600 of Nuclear protein localization protein 4 homolog

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 Nuclear protein localization protein 4 homolog between cysteines 130 and 138.

Details

Redox score ?
90
PDB code
7wwp
Structure name
crystal structure of human npl4
Structure deposition date
2022-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
6
% buried
0
Peptide accession
Q8TAT6
Residue number A
130
Residue number B
138
Peptide name
Nuclear protein localization protein 4 homolog

Ligandability

Cysteine 130 of Nuclear protein localization protein 4 homolog

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 138 of Nuclear protein localization protein 4 homolog

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 Nuclear protein localization protein 4 homolog between cysteines 586 and 589 (9 and 12 respectively in this structure).

Details

Redox score ?
90
PDB code
1nj3
Structure name
structure and ubiquitin interactions of the conserved nzf domain of npl4
Structure deposition date
2002-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
6
% buried
0
Peptide accession
Q9ES54
Residue number A
586
Residue number B
589
Peptide name
Nuclear protein localization protein 4 homolog

Ligandability

Cysteine 586 of Nuclear protein localization protein 4 homolog

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 Nuclear protein localization protein 4 homolog

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 Nuclear protein localization protein 4 homolog between cysteines 138 and 141.

Details

Redox score ?
88
PDB code
7wwp
Structure name
crystal structure of human npl4
Structure deposition date
2022-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
6
% buried
0
Peptide accession
Q8TAT6
Residue number A
138
Residue number B
141
Peptide name
Nuclear protein localization protein 4 homolog

Ligandability

Cysteine 138 of Nuclear protein localization protein 4 homolog

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 141 of Nuclear protein localization protein 4 homolog

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 Nuclear protein localization protein 4 homolog between cysteines 130 and 141.

Details

Redox score ?
86
PDB code
7wwp
Structure name
crystal structure of human npl4
Structure deposition date
2022-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
8
% buried
0
Peptide accession
Q8TAT6
Residue number A
130
Residue number B
141
Peptide name
Nuclear protein localization protein 4 homolog

Ligandability

Cysteine 130 of Nuclear protein localization protein 4 homolog

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 141 of Nuclear protein localization protein 4 homolog

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 Nuclear protein localization protein 4 homolog between cysteines 586 and 603 (9 and 26 respectively in this structure).

Details

Redox score ?
85
PDB code
1q5w
Structure name
ubiquitin recognition by npl4 zinc-fingers
Structure deposition date
2003-08-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
5
% buried
31
Peptide accession
Q9ES54
Residue number A
586
Residue number B
603
Peptide name
Nuclear protein localization protein 4 homolog

Ligandability

Cysteine 586 of Nuclear protein localization protein 4 homolog

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 603 of Nuclear protein localization protein 4 homolog

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 Nuclear protein localization protein 4 homolog between cysteines 600 and 603 (23 and 26 respectively in this structure).

Details

Redox score ?
85
PDB code
1nj3
Structure name
structure and ubiquitin interactions of the conserved nzf domain of npl4
Structure deposition date
2002-12-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
0
Peptide accession
Q9ES54
Residue number A
600
Residue number B
603
Peptide name
Nuclear protein localization protein 4 homolog

Ligandability

Cysteine 600 of Nuclear protein localization protein 4 homolog

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 603 of Nuclear protein localization protein 4 homolog

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 Nuclear protein localization protein 4 homolog between cysteines 341 and 399 (188 and 399 respectively in this structure).

Details

Redox score ?
77
PDB code
7wwq
Structure name
crystal structure of human ufd1-npl4 complex
Structure deposition date
2022-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
16
Peptide accession
Q8TAT6
Residue number A
341
Residue number B
399
Peptide name
Nuclear protein localization protein 4 homolog

Ligandability

Cysteine 341 of Nuclear protein localization protein 4 homolog

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 399 of Nuclear protein localization protein 4 homolog

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 Nuclear protein localization protein 4 homolog between cysteines 589 and 600 (12 and 23 respectively in this structure).

Details

Redox score ?
76
PDB code
1q5w
Structure name
ubiquitin recognition by npl4 zinc-fingers
Structure deposition date
2003-08-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
9
% buried
47
Peptide accession
Q9ES54
Residue number A
589
Residue number B
600
Peptide name
Nuclear protein localization protein 4 homolog

Ligandability

Cysteine 589 of Nuclear protein localization protein 4 homolog

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 600 of Nuclear protein localization protein 4 homolog

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 Nuclear protein localization protein 4 homolog between cysteines 589 and 603 (12 and 26 respectively in this structure).

Details

Redox score ?
68
PDB code
1q5w
Structure name
ubiquitin recognition by npl4 zinc-fingers
Structure deposition date
2003-08-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
44
Peptide accession
Q9ES54
Residue number A
589
Residue number B
603
Peptide name
Nuclear protein localization protein 4 homolog

Ligandability

Cysteine 589 of Nuclear protein localization protein 4 homolog

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 603 of Nuclear protein localization protein 4 homolog

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 Nuclear protein localization protein 4 homolog between cysteines 341 and 391. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
7wwq
Structure name
crystal structure of human ufd1-npl4 complex
Structure deposition date
2022-02-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
98
Minimum pKa ?
13
% buried
100
Peptide accession
Q8TAT6
Residue number A
341
Residue number B
391
Peptide name
Nuclear protein localization protein 4 homolog

Ligandability

Cysteine 341 of Nuclear protein localization protein 4 homolog

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 391 of Nuclear protein localization protein 4 homolog

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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