ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cullin-associated NEDD8-dissociated protein 1

Intramolecular
Cysteine 264 and cysteine 275
Cysteine 264 and cysteine 301
Cysteine 940 and cysteine 942
Cysteine 453 and cysteine 454
Cysteine 571 and cysteine 592
Cysteine 275 and cysteine 356
Cysteine 264 and cysteine 356
Cysteine 275 and cysteine 301
Cysteine 454 and cysteine 500
A redox-regulated disulphide may form within Cullin-associated NEDD8-dissociated protein 1 between cysteines 264 and 275.

Details

Redox score ?
70
PDB code
4a0c
Structure name
structure of the cand1-cul4b-rbx1 complex
Structure deposition date
2011-09-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
7
% buried
82
Peptide accession
Q86VP6
Residue number A
264
Residue number B
275
Peptide name
Cullin-associated NEDD8-dissociated protein 1

Ligandability

Cysteine 264 of Cullin-associated NEDD8-dissociated protein 1

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 275 of Cullin-associated NEDD8-dissociated protein 1

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 Cullin-associated NEDD8-dissociated protein 1 between cysteines 264 and 301 (260 and 297 respectively in this structure).

Details

Redox score ?
69
PDB code
1u6g
Structure name
crystal structure of the cand1-cul1-roc1 complex
Structure deposition date
2004-07-29
Thiol separation (Å)
5
Half-sphere exposure sum ?
66
Minimum pKa ?
7
% buried
60
Peptide accession
Q86VP6
Residue number A
264
Residue number B
301
Peptide name
Cullin-associated NEDD8-dissociated protein 1

Ligandability

Cysteine 264 of Cullin-associated NEDD8-dissociated protein 1

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 301 of Cullin-associated NEDD8-dissociated protein 1

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 Cullin-associated NEDD8-dissociated protein 1 between cysteines 940 and 942. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
1u6g
Structure name
crystal structure of the cand1-cul1-roc1 complex
Structure deposition date
2004-07-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
33
Peptide accession
Q86VP6
Residue number A
940
Residue number B
942
Peptide name
Cullin-associated NEDD8-dissociated protein 1

Ligandability

Cysteine 940 of Cullin-associated NEDD8-dissociated protein 1

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 942 of Cullin-associated NEDD8-dissociated protein 1

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 Cullin-associated NEDD8-dissociated protein 1 between cysteines 453 and 454. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
1u6g
Structure name
crystal structure of the cand1-cul1-roc1 complex
Structure deposition date
2004-07-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
86
Peptide accession
Q86VP6
Residue number A
453
Residue number B
454
Peptide name
Cullin-associated NEDD8-dissociated protein 1

Ligandability

Cysteine 453 of Cullin-associated NEDD8-dissociated protein 1

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 454 of Cullin-associated NEDD8-dissociated protein 1

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 Cullin-associated NEDD8-dissociated protein 1 between cysteines 571 and 592. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4a0c
Structure name
structure of the cand1-cul4b-rbx1 complex
Structure deposition date
2011-09-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
90
Peptide accession
Q86VP6
Residue number A
571
Residue number B
592
Peptide name
Cullin-associated NEDD8-dissociated protein 1

Ligandability

Cysteine 571 of Cullin-associated NEDD8-dissociated protein 1

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 592 of Cullin-associated NEDD8-dissociated protein 1

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 Cullin-associated NEDD8-dissociated protein 1 between cysteines 275 and 356 (271 and 356 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
1u6g
Structure name
crystal structure of the cand1-cul1-roc1 complex
Structure deposition date
2004-07-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
88
Minimum pKa ?
13
% buried
100
Peptide accession
Q86VP6
Residue number A
275
Residue number B
356
Peptide name
Cullin-associated NEDD8-dissociated protein 1

Ligandability

Cysteine 275 of Cullin-associated NEDD8-dissociated protein 1

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 356 of Cullin-associated NEDD8-dissociated protein 1

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 Cullin-associated NEDD8-dissociated protein 1 between cysteines 264 and 356 (260 and 356 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
1u6g
Structure name
crystal structure of the cand1-cul1-roc1 complex
Structure deposition date
2004-07-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
7
% buried
86
Peptide accession
Q86VP6
Residue number A
264
Residue number B
356
Peptide name
Cullin-associated NEDD8-dissociated protein 1

Ligandability

Cysteine 264 of Cullin-associated NEDD8-dissociated protein 1

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 356 of Cullin-associated NEDD8-dissociated protein 1

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 Cullin-associated NEDD8-dissociated protein 1 between cysteines 275 and 301. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
4a0c
Structure name
structure of the cand1-cul4b-rbx1 complex
Structure deposition date
2011-09-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
9
% buried
74
Peptide accession
Q86VP6
Residue number A
275
Residue number B
301
Peptide name
Cullin-associated NEDD8-dissociated protein 1

Ligandability

Cysteine 275 of Cullin-associated NEDD8-dissociated protein 1

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 301 of Cullin-associated NEDD8-dissociated protein 1

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 Cullin-associated NEDD8-dissociated protein 1 between cysteines 454 and 500. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
4a0c
Structure name
structure of the cand1-cul4b-rbx1 complex
Structure deposition date
2011-09-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
98
Peptide accession
Q86VP6
Residue number A
454
Residue number B
500
Peptide name
Cullin-associated NEDD8-dissociated protein 1

Ligandability

Cysteine 454 of Cullin-associated NEDD8-dissociated protein 1

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 500 of Cullin-associated NEDD8-dissociated protein 1

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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