ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Mucolipin-3

Intramolecular
Cysteine 159 and cysteine 185
Cysteine 238 and cysteine 269
Cysteine 417 and cysteine 418
Cysteine 416 and cysteine 417
Cysteine 50 and cysteine 303
Cysteine 296 and cysteine 303
Cysteine 427 and cysteine 429
Cysteine 416 and cysteine 418
Cysteine 427 and cysteine 450
A redox-regulated disulphide may form within Mucolipin-3 between cysteines 159 and 185.

Details

Redox score ?
80
PDB code
5w3s
Structure name
cryo-electron microscopy structure of a trpml3 ion channel
Structure deposition date
2017-06-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
12
Peptide accession
F6RG56
Residue number A
159
Residue number B
185
Peptide name
Mucolipin-3

Ligandability

Cysteine 159 of Mucolipin-3

Cysteine 185 of Mucolipin-3

A redox-regulated disulphide may form within Mucolipin-3 between cysteines 238 and 269.

Details

Redox score ?
62
PDB code
5w3s
Structure name
cryo-electron microscopy structure of a trpml3 ion channel
Structure deposition date
2017-06-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
66
Peptide accession
F6RG56
Residue number A
238
Residue number B
269
Peptide name
Mucolipin-3

Ligandability

Cysteine 238 of Mucolipin-3

Cysteine 269 of Mucolipin-3

A redox-regulated disulphide may form within Mucolipin-3 between cysteines 417 and 418. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
5w3s
Structure name
cryo-electron microscopy structure of a trpml3 ion channel
Structure deposition date
2017-06-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
64
Peptide accession
F6RG56
Residue number A
417
Residue number B
418
Peptide name
Mucolipin-3

Ligandability

Cysteine 417 of Mucolipin-3

Cysteine 418 of Mucolipin-3

A redox-regulated disulphide may form within Mucolipin-3 between cysteines 416 and 417. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
6ayf
Structure name
trpml3/ml-sa1 complex at ph 7
Structure deposition date
2017-09-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
34
Peptide accession
Q8TDD5
Residue number A
416
Residue number B
417
Peptide name
Mucolipin-3

Ligandability

Cysteine 416 of Mucolipin-3

Cysteine 417 of Mucolipin-3

A redox-regulated disulphide may form within Mucolipin-3 between cysteines 50 and 303. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6ayf
Structure name
trpml3/ml-sa1 complex at ph 7
Structure deposition date
2017-09-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
64
Peptide accession
Q8TDD5
Residue number A
50
Residue number B
303
Peptide name
Mucolipin-3

Ligandability

Cysteine 50 of Mucolipin-3

Cysteine 303 of Mucolipin-3

A redox-regulated disulphide may form within Mucolipin-3 between cysteines 296 and 303. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6ayf
Structure name
trpml3/ml-sa1 complex at ph 7
Structure deposition date
2017-09-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
70
Peptide accession
Q8TDD5
Residue number A
296
Residue number B
303
Peptide name
Mucolipin-3

Ligandability

Cysteine 296 of Mucolipin-3

Cysteine 303 of Mucolipin-3

A redox-regulated disulphide may form within Mucolipin-3 between cysteines 427 and 429. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6ayg
Structure name
human apo-trpml3 channel at ph 4
Structure deposition date
2017-09-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
58
Peptide accession
Q8TDD5
Residue number A
427
Residue number B
429
Peptide name
Mucolipin-3

Ligandability

Cysteine 427 of Mucolipin-3

Cysteine 429 of Mucolipin-3

A redox-regulated disulphide may form within Mucolipin-3 between cysteines 416 and 418. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
5w3s
Structure name
cryo-electron microscopy structure of a trpml3 ion channel
Structure deposition date
2017-06-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
12
% buried
86
Peptide accession
F6RG56
Residue number A
416
Residue number B
418
Peptide name
Mucolipin-3

Ligandability

Cysteine 416 of Mucolipin-3

Cysteine 418 of Mucolipin-3

A redox-regulated disulphide may form within Mucolipin-3 between cysteines 427 and 450. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
5w3s
Structure name
cryo-electron microscopy structure of a trpml3 ion channel
Structure deposition date
2017-06-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
100
Peptide accession
F6RG56
Residue number A
427
Residue number B
450
Peptide name
Mucolipin-3

Ligandability

Cysteine 427 of Mucolipin-3

Cysteine 450 of Mucolipin-3

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