Lanosterol synthase
Intramolecular
Cysteine 584 and cysteine 636
Cysteine 567 and cysteine 598
Cysteine 609 and cysteine 616
Cysteine 410 and cysteine 471
Cysteine 653 and cysteine 676
Cysteine 231 and cysteine 449
Cysteine 231 and cysteine 233
Cysteine 449 and cysteine 456
Cysteine 456 and cysteine 533
1w6k A 584 A 636
A redox-regulated disulphide may form within Lanosterol synthase between cysteines 584 and 636.
Details
Redox score ?
65
PDB code
1w6k
Structure name
structure of human osc in complex with lanosterol
Structure deposition date
2004-08-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
10
% buried
100
Peptide accession
P48449
Residue number A
584
Residue number B
636
Peptide name
Lanosterol synthase
Ligandability
Cysteine 584 of Lanosterol synthase
Cysteine 636 of Lanosterol synthase
1w6k A 567 A 598
A redox-regulated disulphide may form within Lanosterol synthase between cysteines 567 and 598. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
1w6k
Structure name
structure of human osc in complex with lanosterol
Structure deposition date
2004-08-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
96
Peptide accession
P48449
Residue number A
567
Residue number B
598
Peptide name
Lanosterol synthase
Ligandability
Cysteine 567 of Lanosterol synthase
Cysteine 598 of Lanosterol synthase
1w6k A 609 A 616
A redox-regulated disulphide may form within Lanosterol synthase between cysteines 609 and 616. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
1w6k
Structure name
structure of human osc in complex with lanosterol
Structure deposition date
2004-08-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
64
Peptide accession
P48449
Residue number A
609
Residue number B
616
Peptide name
Lanosterol synthase
Ligandability
Cysteine 609 of Lanosterol synthase
Cysteine 616 of Lanosterol synthase
1w6k A 410 A 471
A redox-regulated disulphide may form within Lanosterol synthase between cysteines 410 and 471. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
1w6k
Structure name
structure of human osc in complex with lanosterol
Structure deposition date
2004-08-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
68
Peptide accession
P48449
Residue number A
410
Residue number B
471
Peptide name
Lanosterol synthase
Ligandability
Cysteine 410 of Lanosterol synthase
Cysteine 471 of Lanosterol synthase
1w6k A 653 A 676
A redox-regulated disulphide may form within Lanosterol synthase between cysteines 653 and 676. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
1w6k
Structure name
structure of human osc in complex with lanosterol
Structure deposition date
2004-08-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
11
% buried
85
Peptide accession
P48449
Residue number A
653
Residue number B
676
Peptide name
Lanosterol synthase
Ligandability
Cysteine 653 of Lanosterol synthase
Cysteine 676 of Lanosterol synthase
1w6k A 231 A 449
A redox-regulated disulphide may form within Lanosterol synthase between cysteines 231 and 449. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
1w6k
Structure name
structure of human osc in complex with lanosterol
Structure deposition date
2004-08-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
100
Peptide accession
P48449
Residue number A
231
Residue number B
449
Peptide name
Lanosterol synthase
Ligandability
Cysteine 231 of Lanosterol synthase
Cysteine 449 of Lanosterol synthase
1w6k A 231 A 233
A redox-regulated disulphide may form within Lanosterol synthase between cysteines 231 and 233. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
1w6k
Structure name
structure of human osc in complex with lanosterol
Structure deposition date
2004-08-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
13
% buried
100
Peptide accession
P48449
Residue number A
231
Residue number B
233
Peptide name
Lanosterol synthase
Ligandability
Cysteine 231 of Lanosterol synthase
Cysteine 233 of Lanosterol synthase
1w6k A 449 A 456
A redox-regulated disulphide may form within Lanosterol synthase between cysteines 449 and 456. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
26
PDB code
1w6k
Structure name
structure of human osc in complex with lanosterol
Structure deposition date
2004-08-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
88
Minimum pKa ?
11
% buried
100
Peptide accession
P48449
Residue number A
449
Residue number B
456
Peptide name
Lanosterol synthase
Ligandability
Cysteine 449 of Lanosterol synthase
Cysteine 456 of Lanosterol synthase
1w6k A 456 A 533
A redox-regulated disulphide may form within Lanosterol synthase between cysteines 456 and 533. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
22
PDB code
1w6k
Structure name
structure of human osc in complex with lanosterol
Structure deposition date
2004-08-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
92
Minimum pKa ?
15
% buried
100
Peptide accession
P48449
Residue number A
456
Residue number B
533
Peptide name
Lanosterol synthase
Ligandability
Cysteine 456 of Lanosterol synthase
Cysteine 533 of Lanosterol synthase
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